Isolation and identification of a collagenolytic enzyme from the venom of the western diamondback rattlesnake (Crotalus atrox).
A collagenolytic enzyme, with a molecular weight of 58,000 daltons and isoelectric point of 5.1, was isolated and purified from the venom of the rattlesnake Crotalus atrox by Sephadex G-100 gel filtration followed by chromatography on DEAE-Bio-gel A. The enzyme released alpha-chains from beta-chains of the native collagen and cleaved in the helical region similar to other animal collagenases. The enzyme also hydrolyzed the PZ-peptide, however, it did not hydrolyze synthetic substrates for serine protease (such as TAME or ATEE). The enzyme had no hemorrhagic activity. Immunocross-reactivity suggested that only the venom from Crotalidae contain the enzyme.
D000596:Amino Acids / Q000032:analysis; D003429:Cross Reactions; D003435:Crotalid Venoms / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D007120:Immunochemistry; D007525:Isoelectric Focusing; D003012:Microbial Collagenase / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis
D000596:Amino Acids; D003435:Crotalid Venoms; D011506:Proteins; D003012:Microbial Collagenase