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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1994-4-22
|
| pubmed:abstractText |
1. Fibrinogenase was isolated from Candida albicans NH-1 by DEAE-Cellulose, Sephadex G-75 and Sephadex G-100 column chromatographies. 2. The purified fibrinogenase gave a single band on disc polyacrylamide gel electrophoresis, isoelectric focusing and sodium dodecyl sulfate polyacrylamide gel electrophoresis. 3. The enzyme preparation had a molecular weight of 13,000, isoelectric point of pH 4.2 and possessed 117 amino acid residues. 4. The purified fibrinogenase possessed capillary permeability-increasing activity. 5. The enzyme hydrolyzed fibrinogen, casein, hide powder azure, azocoll hydrolytic activities and also hydrolyzed the oxidized B chain of insulin. The cleavage sites in the oxidized B chain of insulin were identified as Asp(3)-Glu(4), Glu(13)-Ala(14), Ala(14)-Leu(15), Tyr(16)-Leu(17), Arg(22)-Gly(23), Phe(25)-Tyr(26) and Tyr(26)-Thr(27). 6. Fibrinogenase activity of this preparation was inhibited by alpha 2-macroglobulin antithrombin-III, o-phenanthroline, disodium ethylenediaminetetra acetic acid and dithiothreitol.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0020-711X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
25
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1815-22
|
| pubmed:dateRevised |
2000-12-18
|
| pubmed:meshHeading | |
| pubmed:year |
1993
|
| pubmed:articleTitle |
Isolation and characterization of fibrinogenase from Candida albicans NH-1.
|
| pubmed:affiliation |
Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
|
| pubmed:publicationType |
Journal Article
|