Endonuclease from Proteus mirabilis | Endonukleaza Proteus mirabilis.

dc.contributor.author	Salikhova Z.
dc.contributor.author	Sokolova R.
dc.contributor.author	Ponomareva A.
dc.contributor.author	Iusupova D.
dc.date.accessioned	2018-09-17T20:45:42Z
dc.date.available	2018-09-17T20:45:42Z
dc.date.issued	2001
dc.identifier.issn	0555-1099
dc.identifier.uri	https://dspace.kpfu.ru/xmlui/handle/net/134007
dc.description.abstract	Two isoforms of nuclease displaying DNase and RNase activities were found in the culture liquid and periplasm of Proteus mirabilis. The enzyme was isolated from the periplasm and then purified to a functionally homogeneous state. The nuclease was equally potent in cleaving denatured and native DNAs by the endonuclease mechanism and was designated Pm endonuclease. The endonuclease was shown to be a temperature-dependent enzyme with a pH optimum of 10.4-10.6, requiring the presence of bivalent metal ions and inhibited by citrate and ethylenediaminetetraacetate.
dc.relation.ispartofseries	Prikladnaia biokhimiia i mikrobiologiia
dc.title	Endonuclease from Proteus mirabilis \| Endonukleaza Proteus mirabilis.
dc.type	Article
dc.relation.ispartofseries-issue	1
dc.relation.ispartofseries-volume	37
dc.collection	Публикации сотрудников КФУ
dc.relation.startpage	43
dc.source.id	SCOPUS05551099-2001-37-1-SID0035222148

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Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.