[Oxygen binding of myoglobins of diving animals].
作者信息
Korobov V N, Nazarenko V I, Starodub N F
出版信息
Ukr Biokhim Zh (1978). 1992 Mar-Apr;64(2):92-4.
PMID:1413124
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.
摘要
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