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

Authors :
S. V. Perry
D Stone
C. I. Harris
Madeleine F. Hardy
Source :
Biochemical Journal. 120:653-660
Publication Year :
1970
Publisher :
Portland Press Ltd., 1970.

Abstract

1. Adult rabbit skeletal-muscle myosin has been shown to contain 1.0 residue of mono-N-methyl-lysine and 3.3 residues of tri-N-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.

Details

ISSN :
03063283
Volume :
120
Database :
OpenAIRE
Journal :
Biochemical Journal
Accession number :
edsair.doi.dedup.....b959239e5d39ae40d7bbe22dd5f9b91d