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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Knorre DG,Buneva VN,Baram GI,Godovikova TS,Zarytova VF

doi

10.1016/0014-5793(86)80052-7

subject

Has Abstract

pub_date

1986-01-01 00:00:00

pages

64-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)80052-7

journal_volume

194

pub_type

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