Isoforms of Serratia marcescens nuclease. Comparative analysis of substrate specificity

dc.contributor.author	Filimonova M.
dc.contributor.author	Garusov A.
dc.contributor.author	Smetanina T.
dc.contributor.author	Andreeva M.
dc.contributor.author	Bogomolnaya L.
dc.contributor.author	Leshchinskaya I.
dc.date.accessioned	2018-09-17T20:08:32Z
dc.date.available	2018-09-17T20:08:32Z
dc.date.issued	1996
dc.identifier.issn	0006-2979
dc.identifier.uri	https://dspace.kpfu.ru/xmlui/handle/net/133090
dc.description.abstract	Comparative analysis of the specificity of Serratia marcescens nuclease isoforms has been carried out. Mononucleotides separated by anion-exchange chromatography in the presence of 7 M urea from partially hydrolyzed RNA with nucleases Sm1 and Sm2 were identified by reverse-phase HPLC. Both enzymes were found to split phosphodiester bonds at nearly all nucleic acid bases. However, nuclease Sm1 demonstrated preferential cleavage of phosphodiester bonds near uracil and nuclease Sm2 near guanine. A possible role of the N-terminal tripeptide fragment in the nuclease mechanism is discussed.
dc.relation.ispartofseries	Biochemistry (Moscow)
dc.subject	Enzyme isoforms
dc.subject	Nuclease
dc.subject	Serratia marcescens
dc.subject	Substrate specificity
dc.title	Isoforms of Serratia marcescens nuclease. Comparative analysis of substrate specificity
dc.type	Article
dc.relation.ispartofseries-issue	10
dc.relation.ispartofseries-volume	61
dc.collection	Публикации сотрудников КФУ
dc.relation.startpage	1274
dc.source.id	SCOPUS00062979-1996-61-10-SID0007642353

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