Dynamic aspects of affinity labelling as revealed by alkylation and phosphorylation of pancreatic ribonuclease with reactive deoxyribodinucleotide derivatives

FEBS Letters

Godovikova, T.S.¹  Zarytova, V.F.¹  Buneva, V.N.¹  Baram, G.I.¹  Knorre, D.G.¹ 

[1] Institute of Bioorganic Chemistry, Siberian Division of the USSR Academy of Sciences, 630090 Novosibirsk, USSR

关键词: Affinity labeling Biopolymer dynamics Reactive dinucleotide derivative Pancreatic RNase;   

DOI  :  10.1016/0014-5793(86)80052-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Affinity labelling of pancreatic RNase with 4-(N-2-chloroethyl-N-methylamino)benzylamide and (N → P) N-methylimidazolide of d(pTpA) results in the formation of monomodified enzyme derivatives retaining partially enzymatic activity. These data together with some cases described in the literature are considered as suggesting the dynamic nature of the enzyme-reagent complex represented by a set of states differing in the probability of intra-complex reaction. In particular, modification may proceed in a low probability state with an especially favorable mutual orientation of reagent and some protein residue remote from the active site of the enzyme resulting in the removal of the covalently attached reagent moiety from the active center.

【 授权许可】

Unknown