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. 1967 Oct;105(1):361–370. doi: 10.1042/bj1050361

3-Methylhistidine in actin and other muscle proteins

P Johnson 1, C I Harris 1, S V Perry 1
PMCID: PMC1198308  PMID: 6056634

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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