Biological activity and the 3-methylhistidine content of actin and myosin.
1. The 3-methylhistidine content of myosin varies according to muscle type. It is highest in myosin from white skeletal muscle and lower values are obtained from myosin of red skeletal and smooth muscle. 2. The 3-methylhistidine content of actin was similar in all of the types of muscle from which it was isolated. 3. The 3-methylhistidine of rabbit actin is localized in a single tryptic peptide that was readily modified during fractionation procedures. 4. Photo-oxidation studies indicated that the 3-methylhistidine residues are not essential for adeonsine triphosphatase and actin-combining activities of myosin. 5. During photooxidation G-actin lost completely the ability to polymerize to the F form before all the 3-methylhistidine was destroyed.
D000251:Adenosine Triphosphatases / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D010856:Columbidae; D003445:Crustacea; D005260:Female; D006639:Histidine / Q000032:analysis*; D046911:Macromolecular Substances; D051379:Mice; D009124:Muscle Proteins / Q000032:analysis*; D009130:Muscle, Smooth / Q000032:analysis; D009132:Muscles / Q000032:analysis; D010084:Oxidation-Reduction; D010455:Peptides / Q000032:analysis; D010777:Photochemistry; D011817:Rabbits; D014357:Trypsin; D014599:Uterus
D000596:Amino Acids; D046911:Macromolecular Substances; D009124:Muscle Proteins; D010455:Peptides; D006639:Histidine; D014357:Trypsin; D000251:Adenosine Triphosphatases