抄録
The cytochrome oxidase activity of our preparation was investigated and found to be similar to those of preparations obtained in several other laboratories for which different purification procedures were used.
The pH optimum was at 5.62 in McIlvaine's buffer at 0.04M with respect to phosphate, and the maximum specific activity was 5.64 sec.-1/mg. protein/cuvette. Using a Na2HPO4-KH2PO4 buffer system, the highest activity was found at 0.075M at pH 5.95.
The activity was increased by treating cytochrome a with heat, alkali or anionic detergents. Guanidine hydrochloride had the greatest effect, increasing the specific activity to 17.1.
The relationship between the physical state of cytochrome a and its activity was discussed.
