(1) The conversion of hemoglobin-haptoglobin into a precursor of biliverdin by animal liver homogenate is identified as an enzymatic reaction.
(2) The observation of the enzyme activity in different animal tissues has revealed that the activity is high in liver and kidney, and extremely low in spleen.
(3) It has been definitely shown by the use of the cell-fractionation technique that the activity is distributed in the supernatant fraction.
(4) The enzyme kinetics was described by the use of supernatant Table IV. The substrate specificity from the viewpoint of hemoglobin derivatives fraction of the liver homogenate as an enzyme preparation.
(5) In reference to the substrate specificity of this enzyme, it was shown that the initial velocity of the degradation was greater in methemoglobin-haptoglobin
2-2 than in methemoglobin-haptoglobin
2-1 or methemoglobin-haptoglobin
1-1. From the viewpoint of hemoglobin derivatives, it has disclosed that the oxygen uptake is greater in carboxyhemoglobin-haptoglobin
2-1 or in methemoglobin-haptoglobin
2-1 than in oxyhemoglobin-haptoglobin
2-1.
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