Endonuclease from Proteus mirabilis

dc.contributor.author	Salikhova Z.
dc.contributor.author	Sokolova R.
dc.contributor.author	Ponomareva A.
dc.contributor.author	Yusupova D.
dc.date.accessioned	2018-09-17T20:06:00Z
dc.date.available	2018-09-17T20:06:00Z
dc.date.issued	2001
dc.identifier.issn	0003-6838
dc.identifier.uri	https://dspace.kpfu.ru/xmlui/handle/net/133032
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. © 2001 MAIK "Nauka/Interperiodica".
dc.relation.ispartofseries	Applied Biochemistry and Microbiology
dc.title	Endonuclease from Proteus mirabilis
dc.type	Article
dc.relation.ispartofseries-issue	1
dc.relation.ispartofseries-volume	37
dc.collection	Публикации сотрудников КФУ
dc.relation.startpage	36
dc.source.id	SCOPUS00036838-2001-37-1-SID27144471933

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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.