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PMID: 7341247 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Proteolytic digestion studies of chromatin core-histone structure. Identification of the limit peptides of histones H3 and H4.

European journal of biochemistry ·Vol. 119 ·No. 1 ·1981-09-00 ·Pages 67-74

Böhm L, Briand G, Sautière P, Crane-Robinson C

Abstract

Trypsin digestion of chromatin results in a well-defined set of limit peptides (P1--P5) derived from the four core histones. Those from histones H3 and H4 have been identified. P1 is H3 residues 27--129; P4 is H4 residues 18--102 and P5 is H4 residues 20--102. The N-terminal sequences removed correlate well with the regions that undergo post-synthetic acetylation and which show the greatest degree of sequence conservation. Autolytic digestion of chromatin releases a peptide (P1') from H3 representing residues 21--135. The implications of protease digestion for the higher order structure of chromatin are discussed.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Animals Chemical Phenomena Chemistry Chickens Chromatin Histones/isolation & purification Peptide Fragments/isolation & purification Trypsin
Chemicals
Amino Acids Chromatin Histones Peptide Fragments Trypsin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Böhm L
Briand G
Sautière P
Crane-Robinson C
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1981-09-00
Pages
67-74
Language
English
Region
England
NLM ID
0107600
Subset
IM
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