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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-2-23
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pubmed:abstractText |
A 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
1243
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
94-100
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7827114-Agkistrodon,
pubmed-meshheading:7827114-Amino Acid Sequence,
pubmed-meshheading:7827114-Amino Acids,
pubmed-meshheading:7827114-Animals,
pubmed-meshheading:7827114-Cations,
pubmed-meshheading:7827114-Chelating Agents,
pubmed-meshheading:7827114-Chromatography,
pubmed-meshheading:7827114-Enzyme Stability,
pubmed-meshheading:7827114-Fibrin,
pubmed-meshheading:7827114-Fibrinogen,
pubmed-meshheading:7827114-Hemorrhage,
pubmed-meshheading:7827114-Hydrolysis,
pubmed-meshheading:7827114-Metalloendopeptidases,
pubmed-meshheading:7827114-Mice,
pubmed-meshheading:7827114-Mice, Inbred Strains,
pubmed-meshheading:7827114-Molecular Sequence Data,
pubmed-meshheading:7827114-Substrate Specificity,
pubmed-meshheading:7827114-Viper Venoms
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pubmed:year |
1995
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pubmed:articleTitle |
Purification and characterization of a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom.
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pubmed:affiliation |
Department of Chemistry, Faculty of Science, Fukuoka University, Japan.
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pubmed:publicationType |
Journal Article
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