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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 92 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 89 | - |
dc.citation.title | WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.citation.volume | 17 | - |
dc.contributor.author | Jeong, Yong Kee | - |
dc.contributor.author | Park, Jeong Uck | - |
dc.contributor.author | Baek, Hyun | - |
dc.contributor.author | Park, Sunghoon | - |
dc.contributor.author | Kong, In Soo | - |
dc.contributor.author | Kim, Dong Wan | - |
dc.contributor.author | Joo, Woo Hong | - |
dc.date.accessioned | 2023-12-22T12:06:01Z | - |
dc.date.available | 2023-12-22T12:06:01Z | - |
dc.date.created | 2017-06-14 | - |
dc.date.issued | 2001-02 | - |
dc.description.abstract | A fibrinolytic enzyme from Bacillus subtilis BK-17 has been purified to homogeneity by gel-filtration and ion-exchange chromatography. Compared to the crude enzyme extract, the specific activity of the enzyme increased 929-fold with a recovery of 29%. The subunit molecular mass of the purified enzyme was estimated to be 31 kDa by SDS-PAGE. The N-terminal amino acid sequence of the purified fibrinolytic enzyme was: A-Q-S-V-P-Y-G-V-S-Q-I-K-A-P-A-A-H-N. The sequence was highly homologous to the fibrinolytic enzymes nattokinase, subtilisin J and subtilisin E from Bacillus spp. However, there was a substitution of three amino acid residues in the N-terminal sequence. The amidolytic activity of the purified enzyme for several substrates was assessed. In comparison with nattokinase and CK (fibrinolytic enzyme from a Bacillus spp.), which showed strong fibrinolytic activity, the amidolytic activity of the enzyme for the synthetic substrate, kallikrein (H-D-Val-Leu-Arg-pNA, S-2266) increased 2.4- and 11.8-fold, respectively. | - |
dc.identifier.bibliographicCitation | WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY, v.17, no.1, pp.89 - 92 | - |
dc.identifier.doi | 10.1023/A:1016685411809 | - |
dc.identifier.issn | 0959-3993 | - |
dc.identifier.scopusid | 2-s2.0-0035024732 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/25253 | - |
dc.identifier.url | https://link.springer.com/article/10.1023%2FA%3A1016685411809 | - |
dc.identifier.wosid | 000168061500016 | - |
dc.language | 영어 | - |
dc.publisher | KLUWER ACADEMIC PUBL | - |
dc.title | Purification and biochemical characterization of a fibrinolytic enzyme from Bacillus subtilis BK-17 | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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