血合筋肉の化学的研究-7-

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Metmyoglobin (MMb), prepared from the red muscle of tuna, Parathunnus sibi, after SCHMID6), was analyzed electrophoretically by means of the TISELIUS apparatus and it was found that this preparation was not homogeneous except for around the isoelectric point (Fig. 1): in addition to the main component a minute one was discerned, the mobility of which differed from that of tuna methemoglobin (MHb) at any pH (Table 1) and was removed unsuccessfully by repeating recrystallization. Horse heart MMb, tested for reference, behaved in the same way at pH 6.0 (Fig. 2 and Table 1). It is uncertain at present whether this minute or small component is the secondary product from Mb or not. Similarly in cases of MHb's of tuna and horse, were observed plural components, the relative amounts of which were, however, fairly close in contrast with the cases of MMb's. The electrophoretic mobility of tuna MMb is very small at least in the pH region covered in this experiment: e.g., in the phosphate buffer (containing 0.05 M NaCl, ?? /2 0.15, pH 7.3) the mobility of tuna MMb is about one half of horse's, one seventh of carp's8), and one fifth of turtle's9). The isoelectric point of tuna MMb was observed at pH 6.8, which agrees with HUYS, finding11) while that of tuna MHb at pH 5.8 (Fig. 3).
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