Occurrence and formation of the N epsilon-methyl-lysines in myosin and the myofibrillar proteins.

The Biochemical journal ·Vol. 120 ·No. 3 ·1970-12-00 ·Pages 653-60

Hardy MF, Harris CI, Perry SV, Stone D

Abstract

1. Adult rabbit skeletal-muscle myosin has been shown to contain 1.0 residue of mono-N(in)-methyl-lysine and 3.3 residues of tri-N(in)-methyl-lysine per molecule of molecular weight 500000. 2. The methyl-lysines appear to be located in the subfragment 1 portion of the myosin molecule. 3. Methyl-lysines are not present in actin, tropomyosin, inhibitory factor and calcium-sensitizing factor. 4. Enzymic methylation of histidine and lysine residues of myosin has been demonstrated in vitro. 5. The methylation of histidine and lysine of the total myofibrillar protein occurs after peptide-bond synthesis. 6. Although methylated lysines and 3-methyl-histidine could not be detected by analysis of hydrolysates, radiochemical evidence is provided for the presence of these residues in the soluble-protein fraction of rabbit skeletal muscle.

MeSH Terms

Amino Acids/analysis Animals Carbon Isotopes Chromatography

Chemicals

Amino Acids Carbon Isotopes

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Hardy M F

Harris C I

Perry S V

Stone D

References (18)

18 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1200653

Published

1970-12-00

Pages

653-60

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1179647

Subset

External Links

PubMed source DOI: 10.1042/bj1200653 PMC Full Text View journal details

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Occurrence and formation of the N epsilon-methyl-lysines in myosin and the myofibrillar proteins.

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