New metalloendopeptidase of Morganella morganii ZM

dc.contributor.author	Zamaliutdinova N.
dc.contributor.author	Minnullina L.
dc.contributor.author	Sharipova M.
dc.contributor.author	Mardanova A.
dc.date.accessioned	2018-09-18T20:17:49Z
dc.date.available	2018-09-18T20:17:49Z
dc.date.issued	2014
dc.identifier.issn	1068-1620
dc.identifier.uri	https://dspace.kpfu.ru/xmlui/handle/net/138428
dc.description.abstract	© 2014 Pleiades Publishing, Ltd. Proteolytic activity, which is inhibited in the presence of o-phenanthroline, was found in M. morganii ZM. Unlike grimelysin, intracellular proteases of M. morganii ZM actively cleave skeletal muscle actin. Several proteolytic proteins of M. morganii ZM were identified in cells by zymography with gelatin. Individual metalloproteinase (35 kDa) was isolated from the M. morganii ZM cell lysates by ammonium sulphate fractionation and purified by hydrophobic chromatography.
dc.relation.ispartofseries	Russian Journal of Bioorganic Chemistry
dc.subject	alignment
dc.subject	BLASTP
dc.subject	metalloendopeptidase
dc.subject	Morganella morganii
dc.subject	purification
dc.title	New metalloendopeptidase of Morganella morganii ZM
dc.type	Article
dc.relation.ispartofseries-issue	6
dc.relation.ispartofseries-volume	40
dc.collection	Публикации сотрудников КФУ
dc.relation.startpage	628
dc.source.id	SCOPUS10681620-2014-40-6-SID84920414543

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