title: [Oxygen binding of myoglobins of diving animals].
abstract: When studying oxygen binding by myoglobins of diving animals it is shown that half-saturation of myoglobins obtained from the muscles of animals who can stop the external respiration for a long period of time occurs at oxygen strength of 0.62-0.67 mm Hg. Such indices of oxygenation of respiratory hemoprotein of muscles are characteristic of most mammals. Temperature being decreased from 37 to 15 degrees C, myoglobin affinity to oxygen considerably increases.
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: D000818:Animals; D003411:Arvicolinae; D004242:Diving; D008322:Mammals / Q000097:blood*; D008907:Mink; D009211:Myoglobin / Q000378:metabolism*; D010041:Otters; D010100:Oxygen / Q000097:blood*; D011485:Protein Binding; D012119:Respiration / Q000502:physiology; D012377:Rodentia; D013696:Temperature
chemical_list: D009211:Myoglobin; D010100:Oxygen
vernacular_title: Sviazyvanie kisloroda mioglobinami nyriaiushchikh zhivotnykh.