PMID: 6285554Jan 1, 1982Paper

Isolation and identification of a collagenolytic enzyme from the venom of the western diamondback rattlesnake (Crotalus atrox)

Toxicon : Official Journal of the International Society on Toxinology
B S Hong


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.


Aug 15, 1975·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J W Simpson
Aug 15, 1971·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J W SimpsonB M Levy
Aug 1, 1973·Analytical Biochemistry·M B BermanP F Davison
Nov 27, 1974·Biochemical and Biophysical Research Communications·J GrossA H Kang
Jul 1, 1971·Proceedings of the Society for Experimental Biology and Medicine·J W Simpson, L J Rider
Feb 1, 1969·Toxicon : Official Journal of the International Society on Toxinology·A T TuB S Hong
Jun 1, 1966·Toxicon : Official Journal of the International Society on Toxinology·A T TuT Tu
Mar 1, 1966·Toxicology and Applied Pharmacology·A T TuG P James

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