title: [Capacity for autoxidation of myoglobin in man and various semi-aquatic animals].
abstract: Resistance to spontaneous oxidation of oxymyoglobin of man and semi-aquatic animals (beaver, otter, musk-rat) was studied as well as the effect of 2.3-diphosphoglycerate (2.3-DPG) and carnosine on this process. The revealed differences in the autooxidation rate of the studied myoglobins are explained by differences in the conformational state of a protein globule, which more actively protects a heme (in semi-aquatic animals) from spontaneous oxidation under conditions of muscular saturation of cells with oxygen, which is confirmed by the results obtained from the analysis of the universal links of pair amino acid residues which stabilize the protein molecule, 2,3-DPG and carnosine decrease the resistance of myoglobin to autooxidation.
authors.forename: V N
authors.initials: VN
authors.lastname: Korobov
authors.forename: V I
authors.initials: VI
authors.lastname: Nazarenko
authors.forename: N F
authors.initials: NF
authors.lastname: Starodub
mesh_terms: D000663:Amphibians / Q000378:metabolism*; D000818:Animals; D003411:Arvicolinae / Q000378:metabolism*; D002335:Carnivora / Q000378:metabolism*; D002336:Carnosine / Q000494:pharmacology; D004163:Diphosphoglyceric Acids / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D009211:Myoglobin / Q000378:metabolism*; D010041:Otters / Q000378:metabolism*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013045:Species Specificity
chemical_list: D004163:Diphosphoglyceric Acids; D009211:Myoglobin; C017595:oxymyoglobin; D002336:Carnosine
vernacular_title: Sposobnost' k autookisleniiu mioglobina cheloveka i nekotorykh poluvodnykh zhivotnykh.