| an extracellular aminopeptidase from clostridium histolyticum. | an aminopeptidase was isolated from the culture filtrate of clostridium histolyticum and purified to homogeneity. absence of endopeptidase activity in the purified preparation was demonstrated. gel filtration on a calibrated column indicates an apparent molecular weight of 340000 for the native enzyme. gel electrophoresis of the denatured enzyme in the presence of dodecylsulfate in constant acrylamide concentration and in a concentration gradient, resulted in the appearance of a single component ... | 1976 | 4318 |
| extracellular aminopeptidase from clostridium histolyticum. | | 1976 | 13266 |
| application of affinity chromatography to the purification of collagenase for the isolation of insoluble elastin. | clostridium histolyticum collagenase (clostridiopeptidase a, ec 3.4.4.19) was purified by batchwise separation with deae-cellulose followed by affinity chromatography on a column of alkali-treated elastin. the n-terminal amino acid profile of elastin isolated from bovine ligamentum nuchae using this enzyme preparation was compared with that of a duplicate sample purified with a mixture of collagenase i and ii (yoshida, e, and noda, h. (1965) biochim. biopsys. acta 105, 562-574). an approx. three ... | 1975 | 164935 |
| collagenase production by achromobacter iophagus. | achromobacter iophagus produced collagenase (ec 3.4.24.3) when cultured aerobically in buffer containing 5% peptone. the bacterium is non-pathogenic and tests on rabbits indicated that the culture medium was atoxic. the collagenase, which hydrolyzed insoluble and soluble native collagen, was purified by (nh4)2 so4 precipitation, starch block electrophoresis, and gel filtration. it was shown to be serologically distinct from clostridium histolyticum collagenase and to have molecular weight and se ... | 1975 | 165833 |
| the application of collagenase, purified by affintiy chromatography, to the isolation of insoluble elastin from bovine aorta. | clostridium histolyticum collagenase (clostridiopeptidase a, ec 3.4.4.16), purified by affinity chromatography, was applied to the isolation of insoluble elastin from bovine aorta. the extremely low level of n-terminal residues (1.6 mol per 10(6) g of protein) present in this preparation indicated the almost complete lack of hydrolytic damage caused by the isolation procedure. the amino acid profile of the aortic elastin was found to be almost identical to that of insoluble elastin prepared from ... | 1975 | 167862 |
| rabbit corneal damage produced by pseudomonas aeruginosa infection. | gross, light microscopic, and electron microscopic examination of the rabbit corneal destruction produced by experimental pseudomonas aeruginosa infections revealed a combination of acute inflammation and liquefaction necrosis of the cornea. degeneration of the epithelial cells and the start of polymorphonuclear leukocyte infiltration of the cornea occurred initially. these changes were followed by loss of the epithelium, degeneration and loss of the keratocytes and endothelium, loss of the char ... | 1975 | 169202 |
| action of bacterial collagenase on ascaris cuticle collagen. | the collagen from the cuticle of ascaris lumbricoides was digested by clostridium histolyticum collagenase [ec 3.4.24.3] in the presence and absence of cacl2. about 1.2 mumoles of amino groups per mg collagen was liberated when the digestion was performed in the presence of 5 mm cacl2, whereas about 0.5 mumole of amino groups per mg collagen was liberated by digestion in the absence of cacl2. in contrast, cacl2 influenced the extent of hydrolysis of rat tail tendon collagen only slightly. the re ... | 1975 | 175053 |
| chemical characterization and study of the autodigestion of pure collagenase from achromobacter iophagus. | only one collagenase (ec 3.4.24.3) is produced by the non-pathogenic achromobacter iophagus strain. the chromatography of the crude enzyme on de-32 cellulose followed by gel filtration on sephadex g-100 in the presence of 1 m sodium chloride led to the isolation of a homogeneous enzyme. its specific activity (1.642 mukat/mg) represents the highest value ever obtained for a bacterial collagenase. the amino acid composition of a. iophagus collagenase differs from that of clostridium histolyticum m ... | 1976 | 177067 |
| consecutive use of omega-aminoalkylagaroses. resolution and purification of clostripain and collagenase from clostridium histolyticum. | | 1976 | 178310 |
| the effect of calcium chloride on the activity and inhibition of bacterial collagenase. | the enzymatic behavior and inhibition patterns of collagenase of clostridium histolyticum in the presence of 0.5 m and 3.4 mm cacl2 have been examined viscosimetrically. the more concentrated salt was found to enhance the rate of digestion of calfskin collagen when either measured viscosimetrically or colorimetrically by trinitrobenzenesulfonate. however, the rate of digestion of calfskin gelatin is unaffected by 0.5 m cacl2 as determined colorimetrically. calcium chloride also proved to have a ... | 1976 | 178615 |
| cleavage of beta-casein by collagenases from achromobacter iophagus and clostridium histolyticum. | | 1976 | 182537 |
| haemorrhagic and inflammatory properties of collagenase from c. histolyticum. | collagenase from clostridium histolyticum induced haemorrhages when applied to the surface of dog lung; it exerted a similar effect on mouse lung when injected intrathoracically. injected into rat paws, bacterial collagenase induced haemorrhage and oedema. effects of collagenase were prevented by several procedures that inhibit collagenolytic activity (heating at various temperatures and incubation with metal-complexing agents such as edta, penicillamine and dithiothreitol). protein protease inh ... | 1976 | 184702 |
| collagenase enzymes from clostridium: characterization of individual enzymes. | four collagenases have been purified to apparent homogeneity from extracts of clostridium histolyticum and partially characterized. the four purified enzymes are devoid of hydrolytic activity against casein and the synthetic substrate, benzolyarginine naphthylamide, but all retain activity against native collagen. the enzymes are initially spearated by isoelectric focusing where three of the enzymes show distinct isoelectric points: collagenase i = 5.50, collagenase ii = 5.65, and collagenases i ... | 1976 | 184822 |
| change in the stability of tendon collagen during ageing in the reptile, calotes versicolor. a brief note. | age related changes in the digestibility of tendon collagen of the garden lizard, calotes versicolor, were traced using type i collagenase from clostridium histolyticum. collagen from older lizards showed less susceptibility for collagenase digestion than the younger lizards suggesting increased number of cross-linkages comparable with mammals. | 1976 | 186668 |
| proteolytic activation of rat liver adenylate cyclase by a contaminant of crude collagenase from clostridium histolyticum. | treatment of rat liver plasma membranes with various commercial preparations of crude collagenase from clostridium histolyticum at concentrations as low as 1 mug/ml, resulted in activation of the adenylate cyclase system. maximal activation occurred at 50 to 100 mug/ml of collagenase, and promoted a 2- to 3-fold increase in the basal activity as well as in the activities stimulated by catecholamines, glucagon, fluoride, or gtp. this was due to an increase in the maximal velocity of the cyclizing ... | 1977 | 191449 |
| the proteolytic action of bacterial proteases from clostridium histolyticum on bovine fibrinogen. | bacterial proteases from clostridium histolyticum bring about the polymerization of fibrinogen into structured fibres, the period being 9 nm when the ionic strength (i) of the solution is between 0.1 and 0.2. at i=0.3 no polymerization occurs, but the successive actions of bacterial proteases and thrombin induce polymerization, the fibres obtained showing a periodic structure: the major period is 23 nm with two minor striations. the striation pattern is different from that obtained with fibrin ... | 1977 | 193574 |
| specific cleavage of reduced and s-carboxamidomethylated neurophysin ii by the collagenase of clostridium histolyticum. | purified collagenase of clostridium histolyticum was shown to cleave reduced and s-carboxamidomethylated bovine neurophysin between cys-13 and gly-14. the scission resulted in formation of two separable fragments: a smaller peptide arising from residues 1 through 13, and a larger peptide comprising the remainder of the residues of the protein. by dansylation procedures, the smaller peptide was shown to have amino-terminal alanine as expected from the sequence of neurophysin ii, and the larger pe ... | 1978 | 207339 |
| the interaction of collagenase with hydroxyapatite and related materials and enzymatic properties of the adsorbed enzyme. | the commercial collagenase from clostridium histolyticum was adsorbed on hydroxyapatite, on bovine femur shaft and on enamel and dentin powders. the substrate specificity of the adsorbed enzyme tested, with chromophore substrate, azocoll and native collagen, differed from that obtained with the soluble enzyme. the adsorption and the substrate specificity was also dependent on the adsorbent used. a pretreatment of hydroxyapatite with chondroitin sulphate, hyaluronate and dna lowered the adsorptio ... | 1978 | 208720 |
| effects of gentamicin on trypsin, chymotrypsin, and collagenase. | the effects of gentamicin on three proteolytic enzymes were studied. gentamicin was tested at concentrations of 0.5-500 microgram/ml. trypsin was tested at 0.5 microgram/ml using p-tosyl-l-arginine methyl ester and at 0.1 and 0.5 microgram/ml using azocoll as the substrate. chymotrypsin was tested at 0.1 and 0.5 microgram/ml with azocoll. a soluble [14c]collagen assay was used to measure activity of collagenase derived from clostridium histolyticum. the profiles of proteolytic activity vs. genta ... | 1978 | 210240 |
| purification and characterization of a marine bacterial collagenase. | a true collagenase was isolated from the culture fluid of a marine bacterium which has been designated vibrio b-30 (atcc 21250). collagenase production was obtained only in media containing collagen or certain degradation products of collagen. partial purification on deae-cellulose and sephadex g-200 columns produced active enzyme which was free of nonspecific proteases but which contained two collagenases. the two collagenases have the same apparent molecular size, and evidence is presented to ... | 1978 | 210785 |
| age changes in collagen characteristics of bone and skin of a short-lived species of reptile. | decalcified bone collagen of older male garden lizards, calotes versicolor, was less susceptible to digestion by collagenase from clostridium histolyticum than that from younger individuals. in aged skin the percentage solubility and the soluble/insoluble collagen ratio decreased, with a concomitant rise in insoluble and total collagen. collagen/unit area increased with advancing age in both dorsal and ventral skin. these results from a non-mammalian poikilothermic vertebrate provide additional ... | 1978 | 212937 |
| [detection of collagenase in passive haemagglutination using collagen-coated erythrocytes (author's transl)]. | human rheumatoid arthritis (ra) collagenase and bacterial collagenase were shown to agglutinate collagen-coated erythrocytes. native collagens of type i and type ii reacted equally well, while denatured collagens showed less distinct agglutination activity. the sensitivity of the method for the detection of purified bacterial collagenase from clostridium histolyticum is very high (100 pg). it is, however, low for human ra collagenase. the agglutination reaction is not inhibited by concentrations ... | 1978 | 213904 |
| preparation of crude clostridium histolyticum collagenase for therapeutic purposes. | the production of a freeze-dried enzymatic preparation from the category of crude collagenases has been described. the method is based on the utilization of a highly proteolytic clostridium histolyticum strain whose products have more advantageous properties for therapeutic purposes than the products of the strain commonly used as yet. | 1978 | 214494 |
| inhibitor of human collagenase from cultures of human tendon. | a potent inhibitor of human collagenases, released from human tendon explants in culture, has been purified and partially characterized. the tendon inhibitor has an estimated molecular weight of 25,000. it is relatively heat-stable but undergoes loss of activity following exposure to trypsin. it inhibits trypsin-activated rheumatoid synovial collagenase as well as the enzyme obtained from polymorphonuclear leukocytes. no inhibition of collagenase from clostridium histolyticum (clostridiopeptidas ... | 1979 | 218961 |
| some newly characterized collagenases from procaryotes and lower eucaryotes. | chemical and enzymatic properties of four collagenases newly isolated from anaerobic clostridium histolyticum, aerobic achromobacter iophagus, and from two lower eucaryotes, the fungus entomophthora coronata and the insect hypoderma lineatum are reviewed. the problems of their biosynthesis and precursors, namely the effect of induction of collagenase and neutral proteinase in achromobacter by their macromolecular substrates are discussed. the two bacterial collagenases are zn-metallo-enzymes; th ... | 1979 | 220520 |
| differences in the degradation of native collagen by two microbial collagenases. | the early stages of degradation of native collagen by two bacterial collagenases were studied by electron microscopy and by automatic edman degradation. the purified collagenase from clostridium histolyticum was shown to cleave native collagen at several sites, but not progressively from the n-terminus, as had been previously suggested. the homogeneous collagenase from achromobacter iophagus cleaves native collagen preferentially at two sites corresponding to the interbands 33-34 and 41-42. the ... | 1979 | 224860 |
| evaluation of a rapid, sensitive and specific assay for the determination of collagenolytic activity in biological samples. | several methods for the determination of collagenolytic activity were compared from the point of view of sensitivity, selectivity, simplicity and practical value for large numbers of biological samples. a labelled collagen substrate was prepared using [3h]acetic anhydride. the specificity of the assay as well as conditions allowing an optimum detection limit were investigated. the influence of low temperatures, lyophilisation and salt concentration on clostridium histolyticum collagenase have be ... | 1979 | 226285 |
| immunofluorescent study of the spore antigens of proteolytic strains of clostridium botulinum. | by means of the spore fluorescent antibody technique 31 strains of clostridium botulinum types a (18 strains), b (10 strains) and f (3 strains) were found to belong to the same homogeneous group irrespective of their toxigenic types. some strains of this species also cross-reacted with certain strains of clostridium sporogenes types i, ii and iii and clostridium histolyticum type ii. by spore antigenic analysis it was found that clostridium parabotulinum contained two components designated l and ... | 1979 | 379206 |
| clindamycin-associated enterocolitis in guinea pigs: evidence for a bacterial toxin. | experimental enterocolitis was induced in guinea pigs by intraperitoneal injection of clindamycin. specimens of feces were collected daily in phosphate-buffered saline (ph 7.0) and pooled every second day. the pooled samples were centrifuged to remove solids, and the supernatant was sterilized by membrane filtration. the sterile fecal supernatants were then dialyzed for 48 h against two 15-liter changes of phosphate-buffered saline and subsequently tested for toxicity in cultured monolayers of m ... | 1979 | 422233 |
| alpha-clostripain. chemical characterization, activity, and thiol content of the highly active form of clostripain. | a highly active form of clostripain, composed of two polypeptide chains (mr = 43,000 and 12,500), was isolated by hydrophobic chromatography from the culture medium of clostridium histolyticum. it differs in amino acid composition, namely in the value for cyst(e)ine, from that previously reported. the analyses of the separated chains are given. activity is related to the number of free cysteine residues and full activity is obtained only after complete reduction of the disulfide bonds. specific ... | 1979 | 762145 |
| responses of clostridium botulinum type b and e progenitor toxins to some clostridial sulfhydryl-dependent proteases. | sulfhydryl-dependent proteases produced by clostridium botulinum types a, b, and f, clostridium histolyticum, clostridium sporogenes and clostridium perfringens activate preferentially type e over type b progenitor toxin but less efficiently than trypsin. the results explain why activable toxin is demonstrable in culture of a strongly proteolytic type b strain. | 1975 | 1104932 |
| the collagen shield as a collagenase inhibitor and clinical indicator of collagenase activity on the ocular surface. | collagen shields applied to the corneas of patients with bacterial keratitis degrade rapidly, often within a few hours. once treatment brings the infection under control, subsequently applied collagen shields degrade more slowly. in vitro models were established to evaluate the significance of these observations. twenty-four and 72-hour collagen shields were incubated with collagenase from clostridium histolyticum. the in vitro rate of digestion of the shields was directly proportional to the co ... | 1992 | 1313747 |
| inhibition of collagenase by aranciamycin and aranciamycin derivatives. | aranciamycin (1), an anthracycline antibiotic, was found to be an inhibitor of clostridium histolyticum collagenase, with an ic50 = 3.7 x 10(-7) m. elastase and trypsin were not inhibited at concentrations less than or equal to 10(-5) m. a number of aranciamycin derivatives 2-13 were prepared and tested for collagenase inhibition. while loss of activity was found for derivatives modified in the sugar ring or rings b and d of the aglycone, increased potency was found when the tertiary alcohol at ... | 1992 | 1322986 |
| an analysis of the role of collagenase and protease in the enzymatic dissociation of the rat pancreas for islet isolation. | crude clostridium histolyticum collagenase is widely used for the enzymatic degradation of pancreatic extracellular matrix in order to isolate the islets of langerhans. the variable enzymatic composition of crude collagenases is a critical issue which contributes to the poor reproducibility of islet isolation procedures. in this study, the separate contributions of collagenase and protease to the islet isolation process were analysed by testing various combinations of purified collagenase and pu ... | 1992 | 1324862 |
| identification of clostridium histolyticum collagenase hyperreactive sites in type i, ii, and iii collagens: lack of correlation with local triple helical stability. | the class i and ii clostridium histolyticum collagenases (chc) have been used to identify hyperreactive sites in rat type i, bovine type ii, and human type iii collagens. the class i chc attack both collagens at loci concentrated in the n-terminal half of these collagens starting with the site closest to the n-terminus. the class ii chc initiate collagenolysis by attacking both collagens in the interior to produce a mixture of c-terminal 62,000 and a n-terminal 36,000 fragments. both fragments a ... | 1992 | 1325154 |
| kinetics of hydrolysis of type i, ii, and iii collagens by the class i and ii clostridium histolyticum collagenases. | the kinetics of hydrolysis of rat tendon type i, bovine nasal septum type ii, and human placental type iii collagens by class i and class ii clostridium histolyticum collagenases (chc) have been investigated. to facilitate this study, radioassays developed previously for the hydrolysis of these [3h]acetylated collagens by tissue collagenases have been adapted for use with the chc. while the chc are known to make multiple scissions in these collagens, the assays are shown to monitor the initial p ... | 1992 | 1325155 |
| potent inhibition of endopeptidase 24.16 and endopeptidase 24.15 by the phosphonamide peptide n-(phenylethylphosphonyl)-gly-l-pro-l-aminohexanoic acid. | a phosphonamide peptide, n-(phenylethylphosphonyl)-gly-l-pro-l-aminohexanoic acid, previously shown to block clostridium histolyticum collagenases, was examined as a putative inhibitor of endopeptidase 24.16 and endopeptidase 24.15. hydrolysis of two endopeptidase 24.16 substrates, i.e. 3-carboxy-7-methoxycoumarin (mcc)-pro-leu-gly-pro-d-lys-dinitrophenyl (dnp) and neurotensin, were completely and dose-dependently inhibited by the phosphonamide inhibitor with ki values of 0.3 and 0.9 nm respecti ... | 1992 | 1332678 |
| synthesis and collagenase inhibition of new glycosides of aranciamycinone: the aglycon of the naturally occurring antibiotic aranciamycin. | glycosides of aranciamycinone were prepared by glycosylation with sugar acetates and trimethylsilyl triflate in dichloromethane. glycosides of the following sugars were prepared: alpha-l-rhamnopyranose, beta-d-glucopyranose, beta-d-ribopyranose, beta-d-xylopyranose, alpha-l-fucopyranose, 2-azido-2,6-dideoxy-alpha-l-mannopyranose, 2,6-dideoxy-alpha-l-arabino-hexopyranose, 3,6-dideoxy-alpha-l-arabino-hexopyranose, and 4,6-dideoxy-alpha-l-lyxo-hexopyranose. the new glycosides were tested for inhibi ... | 1992 | 1335359 |
| clostridium histolyticum collagenases: a new look at some old enzymes. | seven collagenases denoted by the letters alpha, beta, gamma, delta, epsilon, zeta and eta have been purified to homogeneity from the culture filtrate of clostridium histolyticum. all seven enzymes are zinc proteinases that require calcium ions for activity and have essential carboxyl, tyrosyl and lysyl residues. these enzymes can be divided into two classes on the basis of the sequence homologies in their polypeptide chains, as revealed from a comparison of their tryptic digests. this division ... | 1992 | 1336107 |
| synthesis and characterization of some collagen sequence analogs. | some analogs of natural collagen sequences (773-779) were synthesized. the peptides were hydrolyzed at the gly-ile bond not only by crude collagenase isolated from normal rat liver, but also by the bacterial clostridium histolyticum collagenase. the reason for this unusual cleavage site in the latter case may lie in the unordered secondary structure of the substrates measured by cd spectroscopy. | 1992 | 1417889 |
| limited proteolysis of types i, ii and iii collagens at hyper-reactive sites by clostridium histolyticum collagenase. | | 1992 | 1480013 |
| purification and characterization of the lethal toxin (alpha-toxin) of clostridium septicum. | clostridium septicum lethal (alpha-toxin) was purified and found to be a basic protein (pi 8.4) of approximately 48 kda that is both lethal and hemolytic. the alpha-toxin had a hemolytic activity of approximately 2 x 10(7) hemolytic units per mg and a 50% lethal dose of approximately 10 micrograms/kg of body weight for mice. the alpha-toxin formed concentration-dependent, sodium dodecyl sulfate-resistant aggregates of approximately 230 kda. mice immunized with alpha-toxin showed a significant in ... | 1992 | 1541552 |
| [studies on collagenase inhibitors. iv. inhibitors of bacterial collagenase in coptidis rhizoma]. | a hot aqueous extract of coptidis rhizoma had an inhibitory effect on the bacterial collagenase from clostridium histolyticum. active principles were isolated by silica gel column chromatography from the chcl3 extract. consequently, two inhibitors obtained were identified with the chloride of berberine and coptisine. the concentrations of the berberine and coptisine in the assay mixture to give 50% inhibition (ic50) were 0.73 mm and 0.16 mm, respectively. the type of inhibition by coptisine chlo ... | 1991 | 1662269 |
| effect of divalent metal ions on collagenase from clostridium histolyticum. | the collagenase from clostridium histolyticum (ec 3.4.24.3) degrades type iv collagen with km 32 nm, indicating a high affinity for this substrate. ferrous and ferric ions can inhibit clostridium collagenase. inhibition by fe++ was of the mixed, non-competitive type, with ki 90 microm. the inhibitory effect of fe++ may be due to zn++ displacement from the intrinsic functional center of this metalloprotease, since in the presence of excess amounts of zn++ enzyme activity is retained. this inhibit ... | 1991 | 1663343 |
| [anacollagenase by the action of amitriptyline on clostridium histolyticum collagenase]. | intraperitoneal injection of a mixture of collagenase (300 u) and amitriptyline (laroxyl*, 3 mg) induce no lesions in contrast with the severe effects of collagenase alone. also, a complete resistance to intraperitoneal collagenase injection is observed when preceded by 3 intramuscular injections of the same mixture (associated with freund's incomplete adjuvant). this is due to the development of collagenase antibodies, as demonstrated by nephelometry and immunodiffusion. these facts show that a ... | 1991 | 1666017 |
| changes in the core of the mammalian-pyruvate dehydrogenase complex upon selective removal of the lipoyl domain from the transacetylase component but not from the protein x component. | the dihydrolipoyl transacetylase (e2) component contains a cooh-terminal inner domain (e2i) and an extended nh2-terminal structure, which is composed of two lipoyl domains (the fragment containing both is designated as e2l) and a subunit-binding domain (e2b). the four domains are connected by hinge regions. a subcomplex, composed of an oligomer of e2 subunits, protein x (which also has an nh2-terminal lipoyl domain), and the [pyruvate dehydrogenase]-kinase catalytic and basic subunits (kc and kb ... | 1990 | 2167319 |
| inhibition of clostridium histolyticum collagenases by phosphonamide peptide inhibitors. | several phosphonamide peptides having the general structure r-po(oh)-xaa-yaa-zaa were synthesized and tested for inhibition of clostridium histolyticum collagenase. inhibition was found to depend on the nature of r, xaa, yaa and zaa such that the maximal affinity (ki = 5 nm) was observed when r = p-nitrophenylethyl, xaa = gly, yaa = pro and zaa = 2-aminohexanoic acid; this represents the tightest binding of inhibitor reported to date for any bacterial collagenase. substitution of the p-nitrophen ... | 1990 | 2167850 |
| effect of proteolytic enzymes on transepithelial solute transport. | the effects of proteases on air-space clearance (ac) of small ([14c]sucrose, 342 daltons) and large (125i-neutral dextran, 70,000 daltons) solutes were studied in isolated, fluid-filled hamster lungs that were perfused in a nonrecirculating system. when instilled into the air spaces, porcine pancreatic elastase (0.1-0.4 mg/ml) and bovine pancreatic trypsin (bpt) (0.5-2.0 mg/ml), but neither clostridium histolyticum collagenase (5.0 mg/ml) nor phenylmethylsulfonyl fluoride-inactivated bpt caused ... | 1986 | 2430929 |
| human fibroblast collagenase-alpha-macroglobulin interactions. localization of cleavage sites in the bait regions of five mammalian alpha-macroglobulins. | the interaction between human fibroblast collagenase and five mammalian alpha-macroglobulins (human alpha 2-macroglobulin and pregnancy zone protein, rat alpha 1- and alpha 2-macroglobulin, and rat alpha 1-inhibitor 3) differing in primary and quaternary structure has been investigated. complex formation with each of these alpha-macroglobulins follows the course identified for many other proteinases, i.e. specific limited proteolysis in their bait regions inducing a set of conformational changes ... | 1989 | 2462561 |
| proteinase inhibitory spectrum of mouse murinoglobulin and alpha-macroglobulin. | the interactions of mouse murinoglobulin and alpha-macroglobulin with several proteinases were investigated by filtration and by assays of amidolytic activity towards synthetic substrates in the presence of proteinaceous enzyme inhibitors as well as assays of the inhibition of proteolytic activity. mouse alpha-macroglobulin formed complexes with thrombin, clotting factor xa, plasmin, pancreatic kallikrein, plasma kallikrein, submaxillary gland trypsin-like proteinase, neutrophil elastase, and pa ... | 1989 | 2481676 |
| the ketone cinnamoyl-(1-13c-phe)-cgly-pro-pro is a tetrahedral transition state analog inhibitor of c. histolyticum collagenase. | the ketone cinnamoyl-(1-13c-phe)-cgly-pro-pro [(4-13c-5-cinnamido-4-oxo-6-phenylhexanoyl)-pro-pro 2] competitively inhibits a mixture of collagenases from clostridium histolyticum with a ki of 40 +/- 6 nm. 13c-nmr spectroscopy of the ketone in the presence of this collagenase shows a bound 13c resonance at 102.6 ppm and the resonance of the free ketone at 212 ppm. ketone alone shows no trace (less than 0.5%) of a resonance in the region around 100 ppm. the bound resonance is displaceable by anot ... | 1989 | 2539108 |
| [study on the effect of some group-specific agents on clostridiopeptidase]. | the interaction of clostridiopeptidase of clostridium histolyticum with edc, tnm and ma, the specific reagents for cooh-groups, tyrosine and lysine residues was studied. it was shown that at ph 6.0 edc inactivates the enzyme. the inactivation process follows the pseudo-first order kinetics and is described by a second order rate constant equal to 1 m-1 min-1. the synthetic substrate does not prevent, in practical terms, the enzyme inactivation by edc. at ph 8.0 tnm modifies about 19 tyrosine res ... | 1989 | 2547458 |
| [activation in vivo of the collagenase of clostridium histolyticum by erythromycin lactobionate]. | the authors demonstrate a previously not described increase, in vivo, in a mean proportion of 70%, of the enzymatic activity of the clostridium collagenase in rats by erythromycin lactobionate. the pathogenesis of this phenomenon cannot yet be explained. | 1989 | 2555034 |
| novel method for the preparation of sterile collagen-agarose-plates for isolating collagenolytic bacteria. | an assay method for bacterial collagenase using sterile collagen-agarose plates was developed to isolate collagenolytic bacteria. in order to avoid heat-denaturation of collagen, the plates were made at 37 degrees c mixing microwave-sterilized collagen with low melting point-agarose. sensitivities to various proteases were tested on the plates; it was shown that whereas the collagen in these plates was digested only by the collagenases, the collagen could also be hydrolyzed by other proteolytic ... | 1989 | 2561866 |
| production of human adrenocorticotropin by cleavage of alkaline-phosphatase-derived fusion proteins containing repetitive recognition sequences for collagenases. | recombinant plasmids coding for fusion proteins which consist of human adrenocorticotropin joined to n-terminal sequences of escherichia coli alkaline phosphatase via collagenase-sensitive linkers were constructed and used for the production of these proteins by transformed e. coli cells. it was shown that repetitive linkers of the form -gly-(pro-xaa-gly)n-pro- with n greater than or equal to 2 were cleaved by clostridiopeptidase a (clostridium histolyticum) by orders of magnitude faster than co ... | 1989 | 2573529 |
| protease activity in pancreatic islet isolation by enzymatic digestion. | commercial collagenase* prepared from clostridium histolyticum is widely used in isolation of pancreatic islets. it is known that the enzyme is very impure and that there are substantial variations in effectiveness between batches. our studies suggest that one of the impurities of importance in islet isolation is a protease that has not been very well characterized. comparison of two batches of enzyme, one of which was known to give good yields of islets and the other poor yields, showed that th ... | 1989 | 2642834 |
| enzyme-antibody histochemistry. a method for detection of collagens collectively. | different types of distinct molecular forms of collagen are components of the extracellular matrix in most tissues. the common types can usually be detected by immunohistochemical methods but others may escape detection for lack of specific antisera. however, all these collagens are substrates for the collagenase of clostridium histolyticum. in this report we describe a method that allows the visualization of collagens, collectively, in a tissue preparation. the method is based on the affinity b ... | 1987 | 2820910 |
| purification and properties of collagenase from a streptomyces species. | a collagenase active against native, insoluble collagen was isolated from the culture filtrate of a streptomycete which has been designated streptomyces sp. c-51. collagenase was produced by growing this strain in media containing gelatin. purification by ammonium sulfate fractionation and chromatographies on deae-toyopearl and deae-cellulofine columns produced active enzyme which was free of contaminating proteins, including nonspecific proteinases, but which contained two active subspecies (i ... | 1987 | 2822678 |
| [inhibitory action of methysergide bimaleate on the collagenase of clostridium histolyticum]. | inhibitory effects of methysergide bimaleate on the collagenase of the clostridium histolyticum have been established. having previously shown the inhibitory action of serotonin on this bacterial collagenase, the authors have tested methysergide bimaleate as another inhibitor. after injection in the peritoneum of the rats of methysergide bimaleate and collagenase together, lesions are minimal or absent, in contrast with the dramatic effects of collagenase alone. this shows the antagonist role of ... | 1987 | 2830001 |
| new thiol inhibitors of clostridium histolyticum collagenase. importance of the p3' position. | an extensive series of synthetic mercaptotripeptides (hs-ch2-ch2-co-pro-yaa) was prepared, and the inhibitory constants were determined on the clostridium histolyticum collagenase. among the factors which control the optimal binding of these inhibitors, we found that the presence of a free c-terminal carboxylate group in the position p3' of the compounds is of primary importance. in general, the esterification of this carboxylate group decreased the potency of the inhibitors by two orders of mag ... | 1988 | 2832171 |
| near stoichiometric, irreversible inactivation of bacterial collagenases by o-chloranil (3,4,5,6-tetrachloro-1,2-benzoquinone). | the hydrogen-abstracting quinone derivative 3,4,5,6-tetrachloro-1,2-benzoquinone (o-chloranil) caused a strong, near stoichiometric, irreversible inactivation of the collagenases from bacillus cereus, clostridium histolyticum and achromobacter iophagus. p-chloranil was a weaker inactivator. o-chloranil reacted rapidly with a site that affected substrate binding. amino acid analyses of native and totally inactivated enzymes, and the ph-profile of inactivation suggest that the dissociated form of ... | 1988 | 2837215 |
| ketone-substrate analogues of clostridium histolyticum collagenases: tight-binding transition-state analogue inhibitors. | a series of ketone-substrate analogues has been synthesized for the two classes of collagenases from clostridium histolyticum and shown to be competitive inhibitors. these compounds have sequences that match those of specific peptide substrates for these enzymes. the best inhibitor is the ketone analogue of cinnamoyl-leu-gly-pro-pro, which has a ki value of 18 nm for epsilon-collagenase, a class ii enzyme. this is the tightest binding inhibitor reported for any collagenase to date. plots of log ... | 1988 | 2844227 |
| preparation and reconstitution with divalent metal ions of class i and class ii clostridium histolyticum apocollagenases. | both gamma- and zeta-collagenases from clostridium histolyticum are fully and reversibly inhibited by 1,10-phenanthroline at ph 7.5 in the presence of 10 mm cacl2 with ki values of 0.11 and 0.040 mm, respectively. the inhibition is caused by removal of the single, active-site zn(ii) present in each of these enzymes. the nonchelating analogue 1,5-phenanthroline has no effect on the activity of either enzyme. dialysis of the enzymes in the presence of 1,10-phenanthroline, followed by back dialysis ... | 1988 | 2849991 |
| preparation by direct metal exchange and kinetic study of active site metal substituted class i and class ii clostridium histolyticum collagenases. | active site metal substitutions for both gamma- and zeta-collagenases from clostridium histolyticum have been made by direct metal exchange. the incubation of co(ii), cu(ii), ni(ii), cd(ii), and hg(ii) with these native collagenases results in changes in activity that parallel those observed for the reconstitution of the respective apoenzymes with these metal ions. for both collagenases, the exchange reactions with co(ii) and cu(ii) are complete within 1 min. however, the changes in activity obs ... | 1988 | 2849992 |
| gas chromatography/mass spectrometry of bacterial amines. | bacterial amines were examined by gas chromatography/mass spectrometry. under electron impact all trifluoroacetamides exhibited peaks at m/z 69 due to [cf3]+. many trifluoroacetamides also showed peaks at m/z 97 corresponding to the [cocf3]+ ion fragment. the spectra of n-alkyl and aralkyl trifluoroacetamides were consistent with the spectra and their interpretations in the earlier literature. molecular ions were of low abundance for all alkyl trifluoroacetamides having alkyl chains longer than ... | 1985 | 2931124 |
| substrate specificity of beta-collagenase from clostridium histolyticum. | the substrate specificity of beta-collagenase from clostridium histolyticum has been investigated by measuring the rate of hydrolysis of more than 50 tri-, tetra-, penta-, and hexapeptides covering the p3 to p3' subsites of the substrate. the choice of peptides was patterned after sequences found in the alpha 1 and alpha 2 chains of type i collagen. each peptide contained either a 2-furanacryloyl (fa) or cinnamoyl (cn) group in subsite p2 or the 4-nitrophenylalanine (nph) residue in subsite p1. ... | 1985 | 2982835 |
| purification of nonspecific protease-free collagenase from clostridium histolyticum. | the collagenase (ec 3.4.24.3) produced by the bacterium clostridium histolyticum has been purified free from nonspecific protease contaminants by a two-step procedure. the crude culture medium is chromatographed over heparin-sepharose and sephacryl s-200, and the resulting preparation has no activity versus noncollagenous proteins or n alpha-benzoyl-l-arginine ethyl ester, yet cleaves native thermally reconstituted collagen fibrils quite efficiently (specific activity, 3000 units/mg). the purifi ... | 1985 | 2990251 |
| clostridium histolyticum collagenase: development of new thio ester, fluorogenic, and depsipeptide substrates and new inhibitors. | a new series of thio ester, depsipeptide, and peptide substrates have been synthesized for the bacterial enzyme clostridium histolyticum collagenase. the hydrolysis of the depsipeptide substrate was followed on a ph stat, and thio ester hydrolysis was measured by inclusion of the chromogenic thiol reagent 4,4'-dithiopyridine in the assay mixture. the best thio ester substrate, boc-abz-gly-pro-leu-sch2co-pro-nba, had a kcat/km of 63 000 m-1 s-1, while several shorter thio ester sequences were ina ... | 1985 | 2992578 |
| inhibition of collagenase activity by extracts of bovine ocular tissues. | bovine eyes were dissected and separate pools of lens, lens capsule, cornea and vitreous were extracted in guanidine, subjected to ultrafiltration, and examined for their effects on collagenolytic activity. although lens extract was not inhibitory, the cornea and vitreous both contained inhibitors of collagenase. more inhibition was present in the filtrate of the vitreous than in the retentate, whereas the total amount of inhibition in the cornea was distributed almost equally between the two fr ... | 1985 | 2992886 |
| aldehyde and ketone substrate analogues inhibit the collagenase of clostridium histolyticum. | the collagenase from clostridium histolyticum is a mixture of several collagenases, all of which are zinc metalloproteases. this enzyme catalyzes the cleavage of the x-gly peptide bond in the repeating sequence of collagen: -gly-pro-x-gly-pro-x-. thus the s3, s2, and s1 subsites on the enzyme appear to be occupied by the sequence -gly-pro-x- and the s1', s2', and s3' subsites also by -gly-pro-x-. short peptides up to and including n alpha-acyltetrapeptides containing the repeat sequence do not d ... | 1985 | 3002433 |
| complementary substrate specificities of class i and class ii collagenases from clostridium histolyticum. | the substrate specificities of three class i (beta, gamma, and eta) and three class ii (sigma, epsilon, and zeta) collagenases from clostridium histolyticum have been investigated by quantitating the kcat/km values for the hydrolysis of 53 synthetic peptides with collagen-like sequences covering the p3 through p3 subsites of the substrate. for both classes of collagenases, there is a strong preference for gly in subsites p1' and p3. all six enzymes also prefer substrates that contain pro and ala ... | 1985 | 3002445 |
| mode of hydrolysis of collagen-like peptides by class i and class ii clostridium histolyticum collagenases: evidence for both endopeptidase and tripeptidylcarboxypeptidase activities. | the action of three class i (beta, gamma, and eta) and three class ii (delta, epsilon, and zeta) collagenases from clostridium histolyticum on two series of peptides with collagen-like sequences has been examined. the peptides in the first series all contain 4-nitrophenylalanyl-gly-pro-ala in subsites p1 through p3', but each is successively lengthened in the n-terminal direction by addition of an appropriate residue until subsite p5 is occupied. the second group of peptides all have cinnamoyl-l ... | 1985 | 3002446 |
| use of specific collagenases for the isolation of rat liver cells with preserved lipase activities. | the heparin-releasable neutral lipase (ec 3.1.1.3) from rat liver is inactivated by the common preparations of collagenases (ec 3.4.24.3) used for the isolation of liver cells. we show that two collagenases purified from clostridium histolyticum allow both the complete preservation of this lipolytic activity and a good viability of liver cells isolated by the usual perfusion protocol. | 1986 | 3010771 |
| purification of human collagenases with a hydroxamic acid affinity column. | human collagenase has been isolated from skin fibroblasts and rheumatoid synovium by using an affinity matrix, prepared by coupling pro-leu-gly-nhoh to agarose. following the methodology described herein, the skin enzyme was isolated in two steps in 76% yield and the synovial enzyme was purified in three steps in 71% yield. importantly, each enzyme hydrolyzed collagen into 3/4-1/4 cleavage fragments, indicating that a true collagenase had been isolated. the column was specific for the human enzy ... | 1986 | 3021211 |
| purification and characterization of a streptomycete collagenase. | a soil streptomycete designated as streptomyces sp. a8 produced an extracellular collagen hydrolysing enzyme that appeared to be 'true collagenase' as it degraded native collagen under physiological conditions and cleaved the synthetic hexapeptide 4-phenylazobenzyloxycarbonyl-l-prolyl-l-leucyl-glycyl-l-prolyl-d-a rginine into two tripeptides. the enzyme was purified by diethyl aminoethyl cellulose chromatography and sephadex g-150 gel filtration. the purified enzyme had an apparent molecular wei ... | 1986 | 3023269 |
| collagenase chemonucleolysis via epidural injection. a review of 252 cases. | since 1975, collagenase has been injected into 252 herniated intervertebral discs for treatment of sciatica. highly purified preparations of chinese collagenase were extracted from clostridium histolyticum ch 1093 in lyophylized form, which had a specific collagenolytic activity. it had a wide margin of safety as proven by repeated experiments in dogs by means of intradiscal, extradural, intradural, and intravenous injections. one hundred to two hundred units of collagenase dissolved in 5 ml of ... | 1987 | 3026711 |
| limited proteolysis of type i collagen at hyperreactive sites by class i and ii clostridium histolyticum collagenases: complementary digestion patterns. | the initial proteolytic events in the hydrolysis of rat tendon type i collagen by the class i and ii collagenases from clostridium histolyticum have been investigated at 15 degrees c. sodium dodecyl sulfate-polyacrylamide gel electrophoresis has been used to detect the initial cleavage fragments of both the alpha 1(i) and alpha 2 chains, which migrate at different rates in the buffer system employed. experiments with the class i collagenases indicate that the first cleavage occurs across all thr ... | 1987 | 3032235 |
| purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium bacillus cereus (strain soc 67). | the major collagenolytic proteinase present in the culture filtrate of bacillus cereus (strain soc 67, isolated from the human oral cavity) has been purified to homogeneity by a procedure that comprised concentration of ultrafiltered growth medium on a millipore pttk00005 membrane, precipitation with ammonium sulfate, gel permeation chromatography, chromatofocusing, fast protein liquid chromatography on an anion-exchange column, and finally fast protein liquid chromatography on a gel column. the ... | 1987 | 3040751 |
| immunoenzymology of clostridium histolyticum collagenase. | | 1974 | 4137716 |
| [the action of proteolytic enzymes of clostridium histolyticum and clostridium novyi on human plasma proteins]. | | 1973 | 4147399 |
| the effects of clostridium histolyticum collagenase on amino sugar-containing compound-collagen complexes. | | 1967 | 4175206 |
| [composition of gases emitted by clostridium histolyticum cultivated on sodium thioglycolate media in a vaccuum, after alkalinisation of the medium at the end of culturing]. | | 1974 | 4216432 |
| antibody for collagenase from clostridium histolyticum. | | 1965 | 4285539 |
| isolation and characterization of collagenases i and ii from clostridium histolyticum. | | 1965 | 4285899 |
| purification and partial characterization of collagenolytic enzymes from clostridium histolyticum. | | 1968 | 4297964 |
| pseudocollagenase: a protease from clostridium histolyticum. | | 1968 | 4297969 |
| the properties of molecular fragments obtained on treating calfskin collagen with collagenase from clostridium histolyticum. | | 1968 | 4302777 |
| [observations of potentiation of toxins of clostridium perfringens and clostridium histolyticum]. | | 1967 | 4308692 |
| [effect of clostridium histolyticum collagenase on hexa- and polypeptides]. | | 1970 | 4319428 |
| purification by molecular sieve chromatography on polyacrylamide bio gel p-300 of clostridium histolyticum collagenase. | | 1970 | 4322486 |
| clostridium histolyticum collagenase. ii. partial characterization. | | 1972 | 4340512 |
| isolation by affinity chromatography of neutral proteinase from clostridium histolyticum. | | 1973 | 4348177 |
| presence of collagenase from clostridium histolyticum in gingival sulcal debris of a primitive population. | | 1974 | 4358563 |
| [the effect of actinomyces fradiae 119 proteinases, trypsin and clostridium histolyticum collagenase on insoluble collagen from the achilles tendon]. | | 1973 | 4363287 |
| the interaction of alpha2-macroglobulin with proteinases. binding and inhibition of mammalian collagenases and other metal proteinases. | 1. experiments were performed to determine whether the specific collagenases and other metal proteinases are bound and inhibited by alpha(2)-macroglobulin, as are endopeptidases of other classes. 2. a specific collagenase from rabbit synovial cells was inhibited by human serum. the inhibition could be attributed entirely to alpha(2)-macroglobulin; alpha(1)-trypsin inhibitor was not inhibitory. alpha(2)-macroglobulin presaturated with trypsin or cathepsin b1 did not inhibit collagenase, and pretr ... | 1974 | 4374931 |
| a novel aminopeptidase from clostridium histolyticum. | | 1973 | 4631895 |
| [toxinogenesis and sporulation in clostridium histolyticum]. | | 1965 | 4954005 |
| [composition of the gases produced by clostridium histolyticum cultured in a medium containing thioglycolate]. | | 1966 | 4963926 |
| elastolytic activities of clostridium histolyticum. | | 1970 | 4998030 |
| characterization of a human serum inhibitor of clostridium histolyticum proteinase(s). | normal animal sera inhibit at least one clostridium histolyticum proteinase. an assay procedure based on immune hemolysis was developed for the estimation of this inhibition. this inhibitory activity occurs in various levels in the sera of different animal species. the highest titers have been obtained with rat sera. the inhibitory activity from human serum was isolated and purified 16- to 27-fold by sephadex g-200 gel filtration and diethylaminoethyl cellulose or hydroxylapatite chromatography. ... | 1968 | 5303620 |