Year: 1967
Type: article
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.
Source: Biochemical Journal
DOI: 10.1042/bj1050361
Authors: P. Johnson, C I Harris, S V Perry
Institution: University of Birmingham
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Funder: Muscular Dystrophy Association
OpenAlex ID: W303113995