Abstract
HF3 and bothropasin are P-III hemorrhagic snake venom metalloproteinases (SVMPs) of Bothrops jararaca. The DC protein is composed of the disintegrin-like/cysteine-rich domains derived from the autolysis of P-III SVMPs. Here we describe simplified procedures for the isolation of HF3, bothropasin, the DC protein, and BJ-PI, a novel P-I SVMP. The isolated proteins were identified by mass spectrometry. BJ-PI is a potent caseinolytic enzyme devoid of hemorrhagic activity. HF3, bothropasin and BJ-PI show distinct fibrinogenolytic activities.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Bothrops / physiology*
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Chromatography, Gel
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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Crotalid Venoms / isolation & purification*
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Crotalid Venoms / toxicity
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Electrophoresis, Polyacrylamide Gel
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Hemorrhage / chemically induced
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Hemorrhage / pathology
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Metalloendopeptidases / isolation & purification*
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Metalloendopeptidases / toxicity
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Metalloproteases / isolation & purification*
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Metalloproteases / toxicity
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Mice
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Molecular Sequence Data
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Trypsin / chemistry
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Viper Venoms / enzymology*
Substances
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Crotalid Venoms
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Viper Venoms
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Metalloproteases
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Trypsin
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HF3 protein, Bothrops jararaca
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Metalloendopeptidases
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bothropasin, Bothrops jararaca