3-methylhistidine in actin and other muscle proteins.

The Biochemical journal ·Vol. 105 ·No. 1 ·1967-10-00 ·Pages 361-70

Johnson P, Harris CI, Perry SV

Abstract

1. By the use of the extended elution system for basic amino acid analysis, 3-methylhistidine has been detected in hydrolysates of actin isolated from mammalian, fish and bird skeletal muscle. 2. Evidence is presented to indicate that 3-methylhistidine forms part of the primary structure and that in rabbit actin this residue is restricted to one peptide fraction obtained from the tryptic digest. 3. Rabbit skeletal-muscle actin has a 3-methylhistidine:histidine ratio 1:7.6, indicating a minimum molecular weight of 47600. 4. Adult rabbit myosin contains approximately 2 3-methylhistidine residues/mol. These residues are localized in the heavy meromyosin part of the molecule, and are restricted to the major component obtained after succinylation.

MeSH Terms

Amino Acids/analysis Animals Autoanalysis Chickens Chromatography, Ion Exchange Electrophoresis Histidine/analysis Humans Molecular Weight Muscle Proteins/analysis Peptides/analysis Rabbits Salmonidae Trypsin

Chemicals

Amino Acids Muscle Proteins Peptides Histidine Trypsin

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Johnson P

Harris C I

Perry S V

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31 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1050361

Published

1967-10-00

Pages

361-70

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1198308

Subset

External Links

PubMed source DOI: 10.1042/bj1050361 PMC Full Text View journal details

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3-methylhistidine in actin and other muscle proteins.

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