| purification and characterization of jerdofibrase, a serine protease from the venom of trimeresurus jerdonii snake. | a fibrin(ogen)olytic serine protease from trimeresurus jerdonii venom was identified and purified to sds-polyacrylamide gel electrophoresis homogeneity. it is a single chain polypeptide with a molecular weight of 32kda under reduced condition and 28kda under non-reduced condition, respectively. the venom protease catalysed the hydrolysis of some chromogenic substrates such as s2238, s2160, s2302 and s2251. it degraded bbeta-chain of human fibrinogen preferentially. also the enzyme degraded fibri ... | 2001 | 11306131 |
| biochemical and biological properties of trimeresurus jerdonii venom and characterization of a platelet aggregation-inhibiting acidic phospholipase a2. | several biochemical and biological activities such as phospholipase a2, arginine esterase, proteolytic, l-amino acid oxidase, 5'nucleotidase, acetylcholinesterase, thrombin-like, anticoagulant, and hemorrhagic activities were determined for whole desiccated venom of trimeresurus jerdonii. an acidic phospholipase (named tj-pla2) was purified by anionic exchange chromatography, gel filtration, and reverse phase hplc. tj-pla2 had a molecular weight of 16,000 and a pi of 4.8. tj-pla2 was non-lethal ... | 2002 | 11829058 |
| actions of two serine proteases from trimeresurus jerdonii venom on chromogenic substrates and fibrinogen. | jerdonobin and jerdofibrase are two serine proteases purified from the venom of trimeresurus jerdonii. the michaelis constant k(m) and the catalytic rate constant k(cat) of jerdonobin or jerdofibrase on three chromogenic substrates, h-d-pro-phe-arg-pna (s2302), h-d-phe-pipecolyl-arg-pna (s2238), and h-d-val-leu-lys-pna (s2251) were obtained from lineweaver-burk plots. jerdofibrase could hydrolyze all three substrates, but jerdonobin had no detectable activity on s2251, suggesting a relatively br ... | 2002 | 12091097 |
| characterization and cloning of a novel phospholipase a(2) from the venom of trimeresurus jerdonii snake. | a phospholipase a(2) (pla(2)), called jerdoxin, was isolated from trimeresurus jerdonni snake venom and partially characterized. the protein was purified by three chromatographic steps. sds-polyacrylamide gel electrophoresis in the presence or absence of dithiothreitol showed that it had a molecular mass of 15 kda. jerdoxin had an enzymatic activity of 39.4 micro mol/min/mg towards egg yolk phosphatidyl choline (pc). it induced edema in the footpads of mice. in addition, jerdoxin exhibited indir ... | 2002 | 12220717 |
| l-amino acid oxidase from trimeresurus jerdonii snake venom: purification, characterization, platelet aggregation-inducing and antibacterial effects. | an l-amino acid oxidase (lao), designated as tj-lao, was purified to homogeneity from the venom of trimeresurus jerdonii by sephadex g-100 and q sepharose hp chromatography. the molecular weight of this enzyme was 110 kd as estimated by analytical gel filtration and was 55 kd by sds-polyacrylamide gel electrophoresis, suggesting that the enzyme is composed of two subunits. the enzyme has an absorption spectrum characteristic of flavoproteins, containing 2 moles of fmn per mole of enzyme. the n-t ... | 2002 | 12503878 |
| jerdonase, a novel serine protease with kinin-releasing and fibrinogenolytic activity from trimeresurus jerdonii venom. | a novel kinin-releasing and fibrin(ogen)olytic enzyme termed jerdonase was purified to homogeneity from the venom of trimeresurus jerdonii by deae sephadex a-50 anion exchange, sephadex g-100 (superfine) gel filtration and reverse-phase high performance liquid chromatography (rp-hplc). jerdonase migrated as a single band with an approximate molecular weight of 55 kd under the reduced conditions and 53 kd under the non-reduced conditions. the enzyme was a glycoprotein containing 35.8% neutral car ... | 2003 | 12897962 |
| a new protein structure of p-ii class snake venom metalloproteinases: it comprises metalloproteinase and disintegrin domains. | a new metalloproteinase-disintegrin, named jerdonitin, was purified from trimeresurus jerdonii venom with a molecular weight of 36 kda on sds-page. it dose-dependently inhibited adp-induced human platelet aggregation with ic(50) of 120nm. cdna cloning and sequencing revealed that jerdonitin belonged to the class ii of snake venom metalloproteinases (svmps) (p-ii class). different from other p-ii class svmps, metalloproteinase and disintegrin domains of its natural protein were not separated, con ... | 2003 | 14511668 |
| purification and cloning of cysteine-rich proteins from trimeresurus jerdonii and naja atra venoms. | three 26 kda proteins, named as tj-crvp, na-crvp1 and na-crvp2, were isolated from the venoms of trimeresurus jerdonii and naja atra, respectively. the n-terminal sequences of tj-crvp and na-crvps were determined. these components were devoid of the enzymatic activities tested, such as phospholipase a(2), arginine esterase, proteolysis, l-amino acid oxidase, 5'nucleotidase, acetylcholinesterase. furthermore, these three components did not have the following biological activities: coagulant and a ... | 2003 | 14529736 |
| purification, cloning and biological characterization of a novel disintegrin from trimeresurus jerdonii venom. | a novel disintegrin, jerdonin, was purified from the trimeresurus jerdonii venom by means of gel filtration and reverse phase high pressure liquid chromatography. its coding cdna was also isolated from the venom gland. the jerdonin coding cdna is part of a precursor composed of proprotein, metalloproteinase, and disintegrin domains. from the deduced amino acid sequence, jerdonin is composed of 71 amino acid residues including 12 cysteines and the tripeptide sequence arg-gly-asp (rgd), a well-kno ... | 2004 | 15037031 |
| a novel high molecular weight metalloproteinase cleaves fragment f1 of activated human prothrombin. | a hemorrhagic proteinase, jerdohagin, was purified from trimeresurus jerdonii venom by gel filtration and ion-exchange chromatographies. it was a single chain polypeptide with an apparent molecular weight of 96 kda as estimated by sds-page under the non-reducing and reducing conditions. internal peptide sequencing indicated that it consisted of metalloproteinase, disintegrin-like and cysteine-rich domains and belonged to the class iii snake venom metalloproteinases (class p-iii svmps). like othe ... | 2004 | 15302534 |
| a novel disintegrin, jerdonatin, inhibits platelet aggregation and sperm-egg binding. | a novel disintegrin, jerdonatin, was purified to homogeneity from trimeresurus jerdonii venom by gel filtration and reversed-phase high-pressure liquid chromatography. we isolated the cdna encoding jerdonatin from the snake venom gland. jerdonatin cdna precursor encoded pre-peptide, metalloprotease and disintegrin domain. jerdonatin is composed of 72 amino acid residues including 12 cysteines and the tripeptide sequence arg-gly-asp (rgd), a well-known characteristic of the disintegrin family. mo ... | 2004 | 15364294 |
| molecular characterization of a weak fibrinogen-clotting enzyme from trimeresurus jerdonii venom. | a fibrinogen-clotting enzyme designed as jerdonobin-ii was isolated from the venom of trimeresurus jerdonii. it differed in molecular weight and n-terminal sequence with the previously isolated jerdonobin, a thrombin-like enzyme from the same venom. the enzyme consists of a single polypeptide chain with molecular weights of 30,000 and 32,000 under non-reducing and reducing conditions, respectively. jerdonobin-ii showed weak fibrinogen clotting activity and its activity unit on fibrinogen was cal ... | 2004 | 15683874 |
| cdna cloning and functional expression of jerdostatin, a novel rts-disintegrin from trimeresurus jerdonii and a specific antagonist of the alpha1beta1 integrin. | jerdostatin represents a novel rts-containing short disintegrin cloned by reverse transcriptase-pcr from the venom gland mrna of the chinese jerdons pit viper trimeresurus jerdonii. the jerdostatins precursor cdna contained a 333-bp open reading frame encoding a signal peptide, a pre-peptide, and a 43-amino acid disintegrin domain, whose amino acid sequence displayed 80% identity with that of the kts-disintegrins obtustatin and viperistatin. the jerdostatin cdna structure represents the first co ... | 2005 | 16215260 |
| molecular cloning of albolatin, a novel snake venom metalloprotease from green pit viper (trimeresurus albolabris), and expression of its disintegrin domain. | disintegrins are snake venom-derived, rgd- or kgd-containing peptides that can inhibit integrin-mediated platelet aggregation and cell-matix interactions. the aim of this study is to analyze the full-length cdna sequence of a snake venom metalloprotease (svmp) from green pit viper (trimeresurus albolabris) venom and characterize functions of its disintegrin domain on human platelets. from the primary cdna library of venom glands, a partial sequence of a novel svmp (albolatin) was obtained. using ... | 2007 | 17870140 |
| a unique group of inactive serine protease homologues from snake venom. | a number of inactive serine protease homologues (sphs), which have poorly understood functions, have been identified in invertebrates and vertebrates. recently, several sph transcripts have been reported from snake venom glands, which provide potential new tools for the study of the functions of sphs. herein we report for the first time a snake venom serine protease homologue (svsph) protein, designated as tjsvsph, isolated from the venom of trimeresurus jerdonii. despite its high sequence simil ... | 2008 | 18590752 |
| recombinant expression in human cells of active integrin alpha 1 beta 1-blocking rts-disintegrin jerdostatin. | jerdostatin, an rts short disintegrin cloned from protobothrops jerdonii and recombinantly produced in escherichia coli, is a potent and specific antagonist of the alpha(1)beta(1) integrin. jerdostatin selectively blocked the adhesion of alpha(1)beta(1)-k562 cell to collagens i and iv in vitro and angiogenesis in vivo. here we report the recombinant production of jerdostatin in a mammalian cell system, a prerequisite for developing a conditional transgenic mouse to investigate the effect of syst ... | 2010 | 20674586 |
| jerdonuxin, a novel snaclec (snake c-type lectin) with platelet aggregation activity from trimeresurus jerdonii venom. | serious clinical symptoms of trimeresurus jerdonii bite are mainly caused by abnormalities of blood system. we have previously identified and characterized several bioactive components affecting human blood system, such as serine proteases, metalloproteinases and disintegrins. but few snaclec was characterized in the t. jerdonii venom. in this study, a novel snaclec, named jerdonuxin, was isolated, molecular cloned and characterized as a human platelet agonist. on sds-polyacrylamide gel electrop ... | 2010 | 21040740 |
| a novel platelet glycoprotein ib-binding protein with human platelet aggregation-inhibiting activity from trimeresurus jerdonii venom. | platelet glycoprotein ib (gpib) is a primary adhesion receptor and involved in platelet-related disorders. however, it is difficult to study gpib-specific platelet stimulation using physiological ligands in vivo. gpib-binding snake c-type lectins (snaclecs) are useful tools for exploring gpib in vitro because they act on platelets differently. in the present study, a novel gpib-binding snaclec, named jerdonibitin, was purified, molecular cloned and characterized from trimeresurus jerdonii venom. ... | 2011 | 21256857 |
| cdna cloning of a snake venom metalloproteinase from the eastern diamondback rattlesnake (crotalus adamanteus), and the expression of its disintegrin domain with anti-platelet effects. | a 5' truncated snake venom metalloproteinase was identified from a cdna library constructed from venom glands of an eastern diamondback rattlesnake (crotalus adamanteus). the 5'-rapid amplification of cdna ends (race) was used to obtain the 1865 bp full-length cdna sequence of a snake venom metalloproteinase (camvmpii). camvmpii encodes an open reading frame of 488 amino acids, which includes a signal peptide, a pro-domain, a metalloproteinase domain, a spacer, and an rgd-disintegrin domain. the ... | 2013 | 23313448 |
| vascular endothelial growth factor from trimeresurus jerdonii venom specifically binds to vegfr-2. | vascular endothelial growth factors (vegfs) play important roles in angiogenesis. in this study, a vascular endothelial growth factor named tjsvvegf was purified from the venom of trimeresurus jerdonii by gel filtration, affinity, ion-exchange and high-performance liquid chromatography. tjsvvegf was a homodimer with an apparent molecular mass of 29 kda. the cdna encoding tjsvvegf was obtained by pcr. the open reading frame of the cloned tjsvvegf was composed of 432 bp coding for a signal peptide ... | 2015 | 26107411 |
| inhibitory effects of recombinant rts-jerdostatin on integrin α1β1 function during adhesion, migration and proliferation of rat aortic smooth muscle cells and angiogenesis. | jerdostatin, a short rts-disintegrin cloned from venom gland mrna of protobothrops jerdonii, selectively blocks the adhesion of α1β1 integrin to collagen iv. integrin α1β1 is highly expressed in smooth muscle cells (smc) surrounding small blood vessels and vascular endothelial cells. vascular smc adhesion, migration and proliferation are important processes during normal vascular development. using recombinant jerdostatin we have investigated the role of the α1β1 integrin on the adhesion of vasc ... | 2014 | 24418176 |
| mitochondrial genome of protobothrops jerdonii (squamata: viperidae: crotalinae). | protobothrops jerdonii is a common venomous snake that is widely distributed in southwestern china and other adjacent countries of asia. in this study, the complete mitochondrial genome of p. jerdonii was determined. the circle genome with the 17,239 bp total length contained 13 protein-coding genes, 22 transfer rna genes, 2 ribosomal rna genes, and 2 control regions. overall base composition of the complete mtdna was 33.13% a, 25.07% t, 29.31% c, and 12.50% g. all the genes in p. jerdonii were ... | 2013 | 23316752 |
| characterization of a thrombin-like enzyme from the venom of trimeresurus jerdonii. | from the venom of trimeresurus jerdonii, a distinct thrombin-like enzyme, called jerdonobin, was purified by deae a-25 ion-exchange chromatography, sephadex g-75 gel filtration, and fast protein liquid chromatography (fplc). sds-page analysis of this enzyme shows that it consists of a single polypeptide chain with a molecular weight of 38,000. the nh(2)-terminal amino acid sequence of jerdonobin has great homology with venom thrombin-like enzymes documented. jerdonobin is able to hydrolyze sever ... | 2000 | 10736476 |