The effect of pH on the reactions of oxygen and carbon monoxide with the hemoglobin of the carp, Cyprinus carpio.

摘要: Abstract Between pH 8 and 5.6 at 20° the oxygen affinity of carp hemoglobin decreases by a factor more than 100; 5.6, where lowest is found, all heme-heme interaction apparently lost. The kinetic constant which most affected rate dissociation, increases about 100, whereas combination only 3-fold. It appears that properties heme groups molecule are in nearly identical way changes. suggested perhaps low fails to undergo transition high or oxygenated structure remains deoxygenated even when it reacts with oxygen.