title: Preparation and properties of creatine kinase from the breast muscle of normal and dystrophic chicken (Gallus domesticus).
abstract: 1. The purification of creatine kinase from normal and genetically dystrophic chicken breast muscle is described. Enzyme recovery was significantly lower from dystrophic muscle. 2. Both enzymes had the same number of reactive and total thiol groups and had similar specific activities and similar amino acid compositions. 3. No significant differences were observed in sedimentation, electrophoretic or kinetic properties. 4. Peptide ;maps' showed no significant differences, and electrophoresis of partial acid hydrolysates of the labelled enzymes suggested that corresponding amino acid sequences around all the thiol groups were very similar. 5. The enzymes showed identical temperature stabilities. 6. No significant differences between the enzymes from normal and dystrophic muscle were observed.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001345:Autoradiography; D001921:Brain / Q000201:enzymology; D002417:Cattle; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D003402:Creatine Kinase / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D004586:Electrophoresis; D007461:Iodoacetates / Q000494:pharmacology; D007700:Kinetics; D008297:Male; D009132:Muscles / Q000201:enzymology*; D009137:Muscular Dystrophy, Animal / Q000201:enzymology*; D010455:Peptides / Q000032:analysis; D011817:Rabbits; D013438:Sulfhydryl Compounds / Q000032:analysis; D013696:Temperature; D014461:Ultracentrifugation
chemical_list: D000596:Amino Acids; D007461:Iodoacetates; D010455:Peptides; D013438:Sulfhydryl Compounds; D003402:Creatine Kinase