ドジョウの2成分系ヘモグロビンに関する研究-I : 両成分の単離精製および二・三の性質について

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The hemoglobin (Hb) of loach, Misgurnus anguillicaudatus, was previously found1) to consist of two components, which were named F (fast) and S (slow) in accordance with their electrophoretic mobilities. Both components were isolated from each other by starch block electrophoresis and crystallized from concentrated ammonium sulfate solutions (Fig. 1). Some properties of both components were compared to each other. Molecular weights of components F and S were determined to be 74, 000 and 67, 000, respectively, by sedimentation and diffusion method (Table 1). No significant differences were observed between absorption spectrum of both components in the visible region as well as in the near-ultraviolet region (Tables 2 and 3). Comparing with that of horse or tuna Hb, however, the extinction coefficients of SORET bands of both components were characteristically large in met form (Table 2). Both components were electrophoretically homogeneous over all the pH range covered. From the pH vs. mobility curves, isoelectric points of components F and S were found to be at pHs 5.0 and 7.6, respectively (Fig. 2). Such a low isoelectric point of component F has never been reported among vertebrate Hbs11). The solubilities in concentrated phosphate buffer (pH 6.6) of both components were almost the same (Fig. 3). The heat stabilities of the two components were both considerable, component S in cyanmet form being more stable than any of fish Hbs hitherto investigated7) (Fig. 4). As to alkali resistibility, component F was less than S, the difference being wider at higher pH (Fig. 5).

ドジョウの2成分系ヘモグロビンに関する研究-I : 両成分の単離精製および二・三の性質について

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