| isolation of a galactose-binding lectin from the venom of the snake bothrops godmani (godmann's pit viper). | a galactose-binding lectin, isolated from the venom of b. godmani by affinity chromatography, is an acidic protein (pi 4.9) with a subunit mol. wt of about 14,000, occurring mostly as a disulfide-linked dimer of 28,000. a small proportion of lectin appears as a monomer and as a tetramer. the lectin agglutinates erythrocytes from mice, rabbit, cow and human (all abo types, either rh positive or negative), but does not agglutinate horse, sheep, goat and snake (oxybelis aeneus, colubridae) erythroc ... | 1990 | 2109909 |
| chemical modification of histidine and lysine residues of myotoxic phospholipases a2 isolated from bothrops asper and bothrops godmani snake venoms: effects on enzymatic and pharmacological properties. | lysine and histidine residues of two myotoxic phospholipases a2, bothrops asper myotoxin iii and bothrops godmani myotoxin i, were chemically modified in order to study the effects of these treatments on enzymatic and pharmacological properties. after lysine acetylation the overall basicity of these toxins was lost and their enzymatic activity was significantly reduced, although a residual effect remained, which corresponded to 25% of the activity of native toxins. this treatment abolished both ... | 1997 | 9080581 |
| immunochemical properties of the n-terminal helix of myotoxin ii, a lysine-49 phospholipase a(2) from bothrops asper snake venom. | myotoxic class ii phospholipases a(2) from snake venoms can be divided into asp49 and lys49 types. the latter, including bothrops asper myotoxin ii, exert membrane damage despite lacking catalytic activity. a heparin-binding, hydrophobic/cationic region, near the c-terminus of myotoxin ii (115-129) has been shown to be relevant in its membrane-damaging actions. however, some observations suggest also a potential participation of its n-terminal region. an immunochemical approach was utilized to e ... | 2001 | 11137549 |
| modulation of the susceptibility of human erythrocytes to snake venom myotoxic phospholipases a(2): role of negatively charged phospholipids as potential membrane binding sites. | cerrophidion (bothrops) godmani myotoxins i (cgmt-i) and ii (cgmt-ii), asp-49 and lys-49 phospholipases a(2) (pla2s), which drastically differ in enzymatic activity, were devoid of direct hemolytic effects on erythrocytes (rbc) from different species despite the fact that enzymatically active cgmt-i was able to hydrolyze rbc membrane phospholipids and disrupt liposomes prepared from rbc lipids. human rbc did not become susceptible to the toxins after treatment with neuraminidase or after alterin ... | 2001 | 11414685 |
| purification, sequencing, and phylogenetic analyses of novel lys-49 phospholipases a(2) from the venoms of rattlesnakes and other pit vipers. | basic phospholipase a(2) homologs with lys49 substitution at the essential ca(2+)-binding site are present in the venom of pit vipers under many genera. however, they have not been found in rattlesnake venoms before. we have now screened for this protein in the venom of rattlesnakes and other less studied pit vipers. by gel filtration chromatography and rp-hplc, lys49-phospholipase-like proteins were purified from the venoms of two rattlers, crotalus atrox and crotalus m. molossus, and five nonr ... | 2001 | 11594738 |
| snake venomics of the pit vipers porthidium nasutum, porthidium ophryomegas, and cerrophidion godmani from costa rica: toxicological and taxonomical insights. | within the neotropical pit vipers, a lineage of primarily middle american snake species referred to as the "porthidium group" includes the genera atropoides, cerrophidion, and porthidium. in this study, the venom proteomes of porthidium nasutum, p. ophryomegas, and cerrophidion godmani from costa rica were analyzed, and correlated to their toxic and enzymatic activities. their hplc profiles revealed a higher similarity between the two porthidium species than between these and c. godmani. protein ... | 2011 | 22212456 |
| differential susceptibility of c2c12 myoblasts and myotubes to group ii phospholipase a2 myotoxins from crotalid snake venoms. | group ii phospholipase a(2) (pla(2)) myotoxins isolated from viperidae/crotalidae snake venoms induce a rapid cytolytic effect upon diverse cell types in vitro. previous studies suggested that this effect could be more pronounced on skeletal muscle myotubes than on other cell types, including undifferentiated myoblasts. this study utilized the murine skeletal muscle c2c12 cell line to investigate whether differentiated myotubes are more susceptible than myoblasts, and if this characteristic is s ... | 2016 | 15657942 |
| inhibitory effect of fucoidan on the activities of crotaline snake venom myotoxic phospholipases a(2). | myotoxic phospholipases a(2) account for most of the muscle necrosis that results from envenenomation by crotaline snakes. in this study, we investigated the protective effect of fucoidan, a natural sulfated polysaccharide obtained from the brown seaweed fucus vesiculosus, against the cytotoxic and myotoxic activities of a group of phospholipase a(2) myotoxins from crotaline snake venoms: bothrops asper myotoxins i, ii, iii, and iv, cerrophidion godmani myotoxins i and ii, atropoides nummifer my ... | 2003 | 14599557 |
| crystal structure of myotoxin ii, a monomeric lys49-phospholipase a2 homologue isolated from the venom of cerrophidion (bothrops) godmani. | lys49-phospholipase a2 (lys49-pla2) homologues damage membranes by a ca2+-independent mechanism which does not involve catalytic activity. with the aim of determining the structural basis for this novel activity, we have solved the crystal structure of myotoxin-ii, a lys49-pla2 isolated from the venom of cerrophidion (bothrops) godmani (godmt-ii) at 2.8 a resolution by molecular replacement. the final model has been refined to a final crystallografic residual (rfactor) of 18.8% (rfree = 28.2%), ... | 1999 | 10356281 |
| structural characterization and phylogenetic relationships of myotoxin ii from atropoides (bothrops) nummifer snake venom, a lys49 phospholipase a(2) homologue. | in order to analyze its structure-function relationships, the complete amino acid sequence of myotoxin ii from atropoides (bothrops) nummifer from costa rica was determined. this toxin is a lys49-type phospholipase a(2) (pla(2)) homologue, devoid of catalytic activity, structurally belonging to class iia. in addition to the asp49 --> lys change in the (inactive) catalytic center, substitutions in the calcium-binding loop suggest that its lack of enzymatic activity is due to the loss of ability t ... | 2002 | 12127577 |
| amino acid sequence of a myotoxic lys49-phospholipase a2 homologue from the venom of cerrophidion (bothrops) godmani. | the complete amino acid sequence of myotoxin ii (godmt-ii), a myotoxic phospholipase a2 (pla2) homologue from the venom of the central american crotaline snake cerrophidion (bothrops) godmani, was determined by direct protein sequencing methods. godmt-ii is a class ii pla2 showing a lys instead of asp at position 49. an additional substitution in the calcium binding loop region (asn instead of tyr at position 28) suggests the lack of enzymatic activity observed in this toxin is due to loss of it ... | 1998 | 9659381 |
| isolation and characterization of basic myotoxic phospholipases a2 from bothrops godmani (godman's pit viper) snake venom. | two basic myotoxic phospholipases a2 were purified to homogeneity from the venom of bothrops godmani from costa rica by ion-exchange chromatography on cm-sephadex. they have molecular weights of 14,300 (myotoxin i) and 13,400 (myotoxin ii) and isoelectric points of 8.2 (myotoxin i) and 8.9 (myotoxin ii). they behave as amphiphilic proteins in charge-shift electrophoresis and have similar amino acid compositions. both toxins induce drastic myotoxic effects when injected in the gastrocnemius muscl ... | 1992 | 1524423 |
| two phospholipase a2 inhibitors from the plasma of cerrophidion (bothrops) godmani which selectively inhibit two different group-ii phospholipase a2 myotoxins from its own venom: isolation, molecular cloning and biological properties. | myotoxic phospholipases a(2) (pla(2)s; group ii) account for most of the muscle-tissue damage that results from envenomation by viperid snakes. in the venom of the godman's viper (cerrophidion godmani, formerly bothrops godmani), an enzymically active pla(2) (myotoxin i) and an inactive, lys-49 variant (myotoxin ii) induce extensive muscle damage and oedema. in this study, two distinct myotoxin inhibitor proteins of c. godmani, cgmip-i and cgmip-ii, were purified directly from blood plasma by se ... | 2000 | 10698689 |
| preclinical assessment of a polyspecific antivenom against the venoms of cerrophidion sasai, porthidium nasutum and porthidium ophryomegas: insights from combined antivenomics and neutralization assays. | a polyspecific antivenom is used in central america for the treatment of envenomings by viperid snakes. this antivenom is generated in horses hyperimmunized with a mixture of venoms from bothrops asper, crotalus simus and lachesis stenophrys. the present study analyzed the ability of this antivenom to neutralize the venoms of three central american viperid species of the 'porthidium group', i.e. porthidium nasutum, porthidium ophryomegas and cerrophidion sasai, formerly classified as cerrophidio ... | 2013 | 23313380 |
| molecular evolution and structure-function relationships of crotoxin-like and asparagine-6-containing phospholipases a2 in pit viper venoms. | some myotoxic or neurotoxic pla2s (phospholipases a2) from pit viper venoms contain characteristic n6 substitutions. our survey of the venoms of more than ten pit viper genera revealed that n6-pla2s exist only in limited asian pit vipers of two genera, protobothrops and gloydius, and exist as either monomers or the basic subunits of heterodimers in some new world pit vipers. for the newly identified n6-pla2s, the neuromuscular blocking activities were assayed with the chick biventer cervicis neu ... | 2004 | 15032748 |
| isolation, characterization and molecular cloning of anmip, a new alpha-type phospholipase a2 myotoxin inhibitor from the plasma of the snake atropoides nummifer (viperidae: crotalinae). | a new phospholipase a(2) (pla(2))-inhibitory protein was isolated from the plasma of atropoides nummifer, a crotaline snake from central america. this inhibitor was named anmip, given its ability to neutralize the activity of basic pla(2) myotoxins of its own and related venoms. the cdna of anmip was cloned and sequenced, showing that it belongs to the alpha group of phospholipase a(2) inhibitors (plis). anmip appears as a homotrimer in the native state, held together by non-covalent forces, wit ... | 2007 | 17071122 |