アサクサノリのcytochrome Cの二,三の性質

概要

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Cytochrome c (Cyt) was purified from a red alga, Porphyra tenera, by the procedure shown in Fig. 1. This preparation containing 0.474% iron proved to be homogeneous electrophoretically at various pH's. The visible absorption spectra of this Cyt showed remarkable characteristics, especially in reduced form: in 0.1M acetate buffer of pH 6.0, the extinction coefficient of α maximum (at 553 mμ) was found to be only about 3/4 of that of vertebrate11), in addition to that the whole spectrum shifted towards longer wavelengths than that of vertebrate as pointed out already1); in 0.2 N NaOH, the whole spectrum was found to be very similar to that of vertebrate, both in the positions and in extinction coefficients of maxima or minimum, and the extinction coefficient of α maximum was higher than that in the acetate buffer (Fig. 2 and Table 1). Such a large difference of spectrum as caused by the change in pH seems not yet to have been reported for Cyt from any source. The pH-mobility curve of this protein differed also considerably from that of horse14) as shown in Fig. 3. The isoelectric point of this Cyt was found to be around pH 4, which forms a marked contrast to vertebrate Cyt (above pH 10)10, 14).
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