Literature DB >> 1053046

[Tyrosine residues in histones. Kinetics of histones F1 and F2A1 nitration by tetranitromethane].

S V Shliapnikov, G U Margulis, B O Glotov, E S Severin.   

Abstract

The kinetics of nitration of tyrosine residues in histones F1 and F2a1 by tetranitromethane has been investigated. At low ionic strength and 30-fold molar excess of nitrating agent the nitration reaction results in fast modification of all tyrosine residues in both histones. At the same time the rates of modification of different tyrosine residues in histone F2a1 are not identical and markedly exceed the rate of N-Ac-OEt-Tyr nitration in a model system. The increase of reaction mixture ionic strength causes an increase of modification rates. The differential UV-absorption spectra of histone F1 obtained by temperature perturbation show an abnormal positive characteristic maximum at 286.8 nm. Analysis of the dependence of nitration rates of tyrosine residues in histones in saline solutions upon the ionic strength and of difference UV-absorption spectra of histones leads to a conclusion that there are specific interactions of definite parts of histone polypeptide chains. These interactions may arise from aggregation of histone molecules.

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Year:  1976        PMID: 1053046

Source DB:  PubMed          Journal:  Mol Biol (Mosk)        ISSN: 0026-8984


  1 in total

1.  Histone Hl-DNA interaction. Influence of phosphorylation on the interaction of histone Hl with linear fragmented DNA.

Authors:  B O Glotov; L G Nikolaev; S N Kurochkin; E S Severin
Journal:  Nucleic Acids Res       Date:  1977-04       Impact factor: 16.971

  1 in total

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