スジイルカ筋肉におけるmetmyoglobin還元酵素系に関する研究-2-Ferrimyoglobin reductaseの単離と物理化学的性質〔英文〕

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Using a procedure essentially according to HEGESH's isolation method for human fer-rihemoglobin reductase (FerriHb R), its corresponding enzyme, tentatively named ferrimyo-globin reductase (FerriMb R), was isolated in a highly pure state from the skeletal muscle of blue white dolphin, and compared physico-chemically with the FerriHb R isolated from the erythrocytes of the same animal. The sedimentation and diffusion coefficients were 3.70 S and 6.67×10-7cm2 sec-1, respectively, for the FerriHb R, and 3, 91 S and 5.85×10-7cm2 sec-1, for the FerriMb R. The molecular weights, MS, D of the FerriHb R and FerriMb R were 51, 000 and 65, 000, and Me were 61, 000 and 64, 000, respectively. Their pH-mobility curves also differed from each other. These two reductases were, however, hardly distinguishable from each other, both in possessing an isoelectric point near pH 5 and in exhibiting absorp-tion maxima at 279 and 407nm.
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