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pubmed-article:7827114pubmed:abstractTextA non-hemorrhagic metalloprotease (protease L4) was purified from the venom of Chinese Mamushi (Agkistrodon halys brevicaudus) by gel filtration and anion-exchange chromatography. Protease L4 has the molecular weight of 22,000 and its optimum pH was 8.5. The protein was stable in the pH range of 5-9 and below 40 degrees C. The proteolytic activity was inhibited by metal-chelating agents and some metal ions. Calcium ion activated the activity dose-dependently, but had only a minor effect on the thermal and pH stability. L4 showed fibrinogenase activity, hydrolyzing only the A alpha chain of fibrinogen. The protease cleaved preferentially at the N-terminal of Leu and His residues of some peptides.lld:pubmed
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pubmed-article:7827114pubmed:articleTitlePurification and characterization of a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom.lld:pubmed
pubmed-article:7827114pubmed:affiliationDepartment of Chemistry, Faculty of Science, Fukuoka University, Japan.lld:pubmed
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