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pubmed-article:2044839pubmed:abstractText1. Ac1-Proteinase from the venom of Agkistrodon acutus was isolated in a homogeneous form by a previously published method. 2. Ac1-Proteinase possessed lethal, hemorrhagic, caseinolytic, azocaseinolytic, azoalbumin hydrolytic and hide powder azure hydrolytic activities. 3. The toxin also hydrolyzed the oxidized B chain of insulin and fibrinogen. The cleavage sites in the oxidized B chain of insulin were identified as Ala(14)-Leu(15) and Tyr(16)-Leu(17). The A alpha chain of fibrinogen was digested. 4. Biological properties of Ac1-Proteinase were investigated further and are reported in this paper.lld:pubmed
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pubmed-article:2044839pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:2044839pubmed:articleTitleCharacterization of Ac1-Proteinase from the venom of Agkistrodon acutus (Hundred-pace snake) from Taiwan.lld:pubmed
pubmed-article:2044839pubmed:affiliationDepartment of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.lld:pubmed
pubmed-article:2044839pubmed:publicationTypeJournal Articlelld:pubmed