Hemorrhagic protease from the venom of Calloselasma rhodostoma.
1. A hemorrhagic protease I (HP-I) was isolated from Calloselasma rhodostoma venom by Sephadex G-75, DEAE-Sephacel and Q-Sepharose column chromatographies. 2. Homogeneity was established by the formation of a single band in acrylamide gel electrophoresis. 3. HP-I has a molecular weight of 34,800 and possesses hemorrhagic and proteolytic activities. Both activities are inhibited by ethylenediaminetetraacetic acid (EDTA), 1,10-phenanthroline, ethyleneglycolbis-(beta-aminoethyl ether) N,N'-tetraacetic acid (EGTA), and tetraethylenepentamine (TEP). However neither soybean trypsin inhibitor nor p-chlorobenzoic acid (PCMB) were found to have any effect. 4. The toxin contains 311 amino acid residues and exhibits an isoelectric point of 4.5. 5. The A alpha chain of fibrinogen was cleaved first, followed later by the B beta chain.
Bando
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E
Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
Nikai
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T
Sugihara
H
H
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003094:Collagen / Q000378:metabolism; D003435:Crotalid Venoms / Q000737:chemistry*; D005340:Fibrinogen / Q000378:metabolism; D007328:Insulin / Q000378:metabolism; D008666:Metalloendopeptidases / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013379:Substrate Specificity
D000596:Amino Acids; D003435:Crotalid Venoms; D007328:Insulin; D005340:Fibrinogen; D003094:Collagen; D008666:Metalloendopeptidases; C073275:hemorrhagic protease, Calloselasma rhodostoma