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PMID: 1150664 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The primary structure of actin from rabbit skeletal muscle. Five cyanogen bromide peptides, including the NH2 and COOH termini.

The Journal of biological chemistry ·Vol. 250 ·No. 15 ·1975-08-10 ·Pages 5897-905

Elzinga M, Collins JH

Abstract

As a part of a study of the complete amino acid sequence of actin we have determined the sequences of five cyanogen bromide peptides, which together contain 158 amino acid residues, including the two ends of the molecule. The five peptides are: CB-13 (residues 1 to 44 in the intact chain), CB-11 (residues 83 to 119), CB-12 (residues 228 to 268), CB-8 (residues 283 to 298), and CB-9 (residues 355 to 374). Each of the peptides except CB-11 has one sulfhydryl group, and these peptides thus account for 4 of the 5 cysteines in actin. The reactivity of actin --SH groups toward N-ethylmaleimide was investigated, and it was found that Cys-373 (in CB-9 adjacent to the COOH-terminal phenylalanine) is the first to react with this reagent.

MeSH Terms
Actins Amino Acid Sequence Amino Acids/analysis Aminopeptidases Animals Binding Sites Carboxypeptidases Chromatography, Gel Chromatography, Ion Exchange Chymotrypsin Cyanogen Bromide Ethylmaleimide Muscles/analysis Peptide Fragments/analysis Protein Binding Rabbits Subtilisins Thermolysin Trypsin
Chemicals
Actins Amino Acids Peptide Fragments Carboxypeptidases Aminopeptidases Subtilisins Chymotrypsin Trypsin Thermolysin Ethylmaleimide Cyanogen Bromide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Elzinga M
Collins J H
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1975-08-10
Pages
5897-905
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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