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Purification of recombinant extracellular proteases from Bacillus pumilus for ß-amyloid peptide cleavage

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dc.contributor.author Toymentseva A.
dc.contributor.author Danilova I.
dc.contributor.author Tihonova A.
dc.contributor.author Sharipova M.
dc.contributor.author Balaban N.
dc.date.accessioned 2018-09-19T20:57:53Z
dc.date.available 2018-09-19T20:57:53Z
dc.date.issued 2016
dc.identifier.issn 1068-1620
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/143465
dc.description.abstract © 2016 Pleiades Publishing, Ltd. Using the expression vector pGP382 containing a constitutive promoter (P degQ36 ) and an affinity tag (Strep-tag), we have obtained highly purified recombinant Bacillus pumilus 3-19 proteinases with different substrate specificities: glutamylendopeptidase (GseBp), subtilisin-like protease (AprBp), and metalloendopeptidase (MprBp). The products of the hydrolysis of the ß-amyloid peptide by the bacterial proteases from B. pumilus have been studied. The findings on the potential of the practical application of these bacterial enzymes as the agents preventing the development of the Alzheimer's disease are presented.
dc.relation.ispartofseries Russian Journal of Bioorganic Chemistry
dc.subject affinity chromatography
dc.subject Bacillus pumilus 3-19
dc.subject biological activity
dc.subject expression vector
dc.subject glutamylendopeptidase
dc.subject metalloendopeptidase
dc.subject subtilisin-like protease
dc.title Purification of recombinant extracellular proteases from Bacillus pumilus for ß-amyloid peptide cleavage
dc.type Article
dc.relation.ispartofseries-issue 1
dc.relation.ispartofseries-volume 42
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 53
dc.source.id SCOPUS10681620-2016-42-1-SID84957573145


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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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