|dc.contributor.author||Hyun Sook Lee||-|
|dc.contributor.author||Yung Hee Kho||-|
|dc.contributor.author||Kye Joon Lee||-|
|dc.description.abstract||MAPI (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.title||Inhibition of various proteases by MAPI and inactivation of MAPI by trypsin||-|
|dc.title.alternative||Inhibition of various proteases by MAPI and inactivation of MAPI by trypsin||-|
|dc.citation.title||Journal of Microbiology and Biotechnology||-|
|dc.contributor.affiliatedAuthor||Yung Hee Kho||-|
|dc.identifier.bibliographicCitation||Journal of Microbiology and Biotechnology, vol. 10, no. 2, pp. 181-186||-|
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