[Oxygen binding of myoglobins of diving animals].
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.
Korobov
V N
VN
Nazarenko
V I
VI
Starodub
N F
NF
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
D009211:Myoglobin; D010100:Oxygen
Sviazyvanie kisloroda mioglobinami nyriaiushchikh zhivotnykh.