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Novel extracellular ribonuclease from Bacillus intermedius - binase II: Purification and some properties of the enzyme

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dc.contributor.author Skvortsova M.
dc.contributor.author Bocharov A.
dc.contributor.author Yakovlev G.
dc.contributor.author Znamenskaya L.
dc.date.accessioned 2018-09-17T20:41:02Z
dc.date.available 2018-09-17T20:41:02Z
dc.date.issued 2002
dc.identifier.issn 0320-9725
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/133877
dc.description.abstract The recombinant enzyme binase II was isolated from the culture liquid of Bacillus subtilis 3922 transformed with the pJF28 plasmid bearing the birB gene. The procedure of the enzyme purification included precipitation by polyethylene glycol with subsequent chromatography on DEAE-cellulose, heparin-Sepharose, and Toyopearl TSK-gel. The enzyme was purified 142-fold yielding a preparation with specific activity 1633 U/mg. The molecular weight of binase II is 30 kD. The enzyme is activated by Mg2+ and virtually completely inhibited by EDTA. The pH optimum for the reaction of RNA hydrolysis is 8.5. The properties of the enzyme are close to those of RNase Bsn from B. subtilis. The character of cleaving of synthetic single- and double-stranded polyribonucleotides by binase II suggests that the enzyme binds the substrate in the helix conformation, and its catalytic mechanism is close to that of RNase VI from cobra venom.
dc.relation.ispartofseries Biokhimiya
dc.subject Bacillus intermedius
dc.subject Bacillus subtilis
dc.subject Binase II
dc.subject Biosynthesis
dc.subject Enzyme purification
dc.subject RNase Bsn
dc.title Novel extracellular ribonuclease from Bacillus intermedius - binase II: Purification and some properties of the enzyme
dc.type Article
dc.relation.ispartofseries-issue 7
dc.relation.ispartofseries-volume 67
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 967
dc.source.id SCOPUS03209725-2002-67-7-SID0036410357


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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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