Inhibition of various proteases by MAPI and inactivation of MAPI by trypsin

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dc.contributor.authorHyun Sook Lee-
dc.contributor.authorYung Hee Kho-
dc.contributor.authorKye Joon Lee-
dc.date.accessioned2017-04-19T08:57:30Z-
dc.date.available2017-04-19T08:57:30Z-
dc.date.issued2000-
dc.identifier.issn1017-7825-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5277-
dc.description.abstractMAPI (microbial alkaline protease inhibitor) was isolated from culture broth of Streptomyces chromofuscus SMF28. The K(i) values of MAPI for the representative serine proteases such as chymotrypsin and proteinase K were 0.28 and 0.63 μM, respectively, and for the cysteine proteases cathepsin B and papain were 0.66 and 0.28 μM, respectively. These data indicate that MAPI is not a potent selective inhibitor of serine or cysteine proteases. Progress curves for the inhibition of three proteases by MAPI exhibited characteristic patterns: MAPI exhibited slow-binding inhibition of cathepsin B. It was rapidly associated with chymotrypsin before the addition of substrate and then reactivation of MAPI-inhibited enzyme was investigated in the presence of substrate. On the other hand, MAPI-proteinase K interaction was typical for those classical inhibitors. When MAPI was incubated with trypsin, there was an extensive reduction in the inhibitory activities of MAPI corresponding to 66.5% inactivation of MAPI, indicating that trypsin- like protease may play a role in the decrease of the inhibitory activity during cultivation.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleInhibition of various proteases by MAPI and inactivation of MAPI by trypsin-
dc.title.alternativeInhibition of various proteases by MAPI and inactivation of MAPI by trypsin-
dc.typeArticle-
dc.citation.titleJournal of Microbiology and Biotechnology-
dc.citation.number2-
dc.citation.endPage186-
dc.citation.startPage181-
dc.citation.volume10-
dc.contributor.affiliatedAuthorYung Hee Kho-
dc.contributor.alternativeName이현숙-
dc.contributor.alternativeName고영희-
dc.contributor.alternativeName이계준-
dc.identifier.bibliographicCitationJournal of Microbiology and Biotechnology, vol. 10, no. 2, pp. 181-186-
dc.subject.keywordMAPI-
dc.subject.keywordStreptomyces chromofuscus-
dc.subject.keywordslow-binding inhibition-
dc.subject.keywordinactivating enzyme-
dc.subject.keywordtrypsin-like protease-
dc.subject.localMAPI-
dc.subject.localStreptomyces chromofuscus-
dc.subject.localslow-binding inhibition-
dc.subject.localinactivating enzyme-
dc.subject.localtrypsin-like protease-
dc.description.journalClassY-
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