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Chitinolytic complex of serratia marcescens and peculiarities of its biosynthesis

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dc.contributor.author Porfir'eva O.
dc.contributor.author Yusupova D.
dc.contributor.author Zotkina N.
dc.contributor.author Sokolova R.
dc.contributor.author Gabdrakhmanova L.
dc.date.accessioned 2018-09-17T20:28:15Z
dc.date.available 2018-09-17T20:28:15Z
dc.date.issued 1997
dc.identifier.issn 0026-3656
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/133531
dc.description.abstract The extracellular chitinolytic complex of Serratia marcescens Bu 211 ATCC 9986 was shown to include three proteins with molecular masses of 52, 52, and 45 kDa (chitinases A, B, and C, respectively). Chitinases A and B were separated from chitinase C and purified from protein admixtures by chromatography on chitin. Chitinase A possessed two isoforms with pi values of 6.25 and 4.85-5.25. Chitinase B had only one isoform with a pi of 4.85-5.25 and appeared to be an endochitinase. In the absence of chitin, the biosynthesis of extracellular chitinases was induced by mitomycin C (MC), an inducer of the SOS-response in cells. In the presence of chitin in the cultivation medium, MC increased the chitinase activity. MC induced the synthesis of all three extracellular chitinases, but not of chitobiase, whose biosynthesis was induced by the substrate.
dc.relation.ispartofseries Mikrobiologiya
dc.subject Chitinase
dc.subject Chitobiase
dc.subject Induction
dc.subject Mitomycin c
dc.subject Serratia marcescens
dc.title Chitinolytic complex of serratia marcescens and peculiarities of its biosynthesis
dc.type Article
dc.relation.ispartofseries-issue 3
dc.relation.ispartofseries-volume 66
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 347
dc.source.id SCOPUS00263656-1997-66-3-SID0141708480


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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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