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[核糖核酸酶与5-脱氧核糖核苷酸反应类似物烷基化过程中亲和力修饰的多重性]

[Multiplicity of affinity modification of RNAse during its alkylation with a reactive analog of 5-deoxyribonucleotide].

作者信息

Baram G I, Buneva V N, Dobrikova E Iu, Petrov V N

出版信息

Bioorg Khim. 1986 May;12(5):613-20.

PMID:3730008
Abstract

The interaction of pancreatic RNase with 5'-deoxyribodinucleotide alkylating derivative, 4-(N-2-chloroethyl-N-methylamino)benzylamide of d(pTpA) d[(ClRCH2NH)pTpA], was studied. The unreactive oxyanalogue d[(HORCH2NH)pTpA] was shown to act as competitive inhibitor of cCMP hydrolysis by RNase. d[(ClRCH2NH)pTpA] irreversibly inactivated RNase. A protective effect was exerted by d(pTpA) and d[(HORCH2NH)pTpA]. The modification, although having an affinity character, was not accompanied by total inactivation of the enzyme. It was supposed that covalent bonding between the reagent and enzyme induced the dinucleotide displacement from the recognition site. The formation of four RNase monolabeled forms retaining the activity in the hydrolysis of cCMP and poly(U) was demonstrated.

摘要

研究了胰腺核糖核酸酶与5'-脱氧核糖二核苷酸烷基化衍生物d(pTpA)的4-(N-2-氯乙基-N-甲基氨基)苄基酰胺d[(ClRCH2NH)pTpA]的相互作用。未反应的氧类似物d[(HORCH2NH)pTpA]被证明可作为核糖核酸酶水解cCMP的竞争性抑制剂。d[(ClRCH2NH)pTpA]使核糖核酸酶不可逆地失活。d(pTpA)和d[(HORCH2NH)pTpA]具有保护作用。这种修饰虽然具有亲和特性，但并未导致酶完全失活。据推测，试剂与酶之间的共价键合导致二核苷酸从识别位点位移。已证明形成了四种在cCMP和聚(U)水解中保留活性的核糖核酸酶单标记形式。

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