Purification and partial characterization of a high molecular weight metalloproteinase from the venom of Crotalus adamanteus (eastern diamondback rattlesnake).
Chromatography of Crotalus adamanteus venom on CM-Sepharose, Cibacron Blue-Sepharose and Phenyl-Sepharose, followed by gel filtration on Ultrogel AcA 44, has resulted in the isolation in homogeneous condition of a metalloproteinase active on casein and hide powder azure. The proteinase has an alkaline isoelectric point, and the trivial name proteinase B ('basic proteinase') is suggested to distinguish it from previously characterized C. admanteus metalloproteinases. Proteinase B is a single chain glycoprotein containing one free sulfhydryl group and having a molecular weight of 60,000. Proteinase B was inactivated by treatment with EDTA, but exposure to phenylmethylsulfonyl fluoride had no effect on proteolytic activity. Proteinase B lacked hemorrhagic activity and did not digest chromogenic substrates specific for thrombin, plasmin or plasma kallikrein.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000032:analysis*; D010450:Endopeptidases / Q000032:analysis* / Q000302:isolation & purification; D004950:Esterases / Q000032:analysis; D006470:Hemorrhage / Q000139:chemically induced; D008666:Metalloendopeptidases; D051379:Mice; D008813:Mice, Inbred ICR; D008970:Molecular Weight
D000596:Amino Acids; D003435:Crotalid Venoms; D004950:Esterases; D010450:Endopeptidases; D008666:Metalloendopeptidases