3-methylhistidine in actin and other muscle proteins.
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.
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D001322:Autoanalysis; D002645:Chickens; D002852:Chromatography, Ion Exchange; D004586:Electrophoresis; D006639:Histidine / Q000032:analysis*; D006801:Humans; D008970:Molecular Weight; D009124:Muscle Proteins / Q000032:analysis*; D010455:Peptides / Q000032:analysis; D011817:Rabbits; D012487:Salmonidae; D014357:Trypsin
D000596:Amino Acids; D009124:Muscle Proteins; D010455:Peptides; D006639:Histidine; D014357:Trypsin