STUDIES ON MULTIPLE HEMOGLOBINS OF EEL-I:ABSORPTION SPECTRUM AND SOME OTHER PROPERTIES

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The hemoglobin (Hb) of eel, Anguilla japonica, was electrophoretically found to consist of a fast component (named F, but whether this component may be separated further into two or more components or not, is not clear at present) and a slow one (named S). Both components were successfully crystallized after isolation either by starch block electrophoresis or by CMC column chromatography (Fig. 1), and were compared to each other in respect of some characteristics. Absorption spectra of component F in met form in visible region, as well as in most derivatives in near-ultraviolet region, were located at longer wavelengths than those of component S or mammalian Hb's (Figs. 2 and 3, Tables 1 and 2). It was also noticed that extinction coefficients of component F at absorption maxima were extremely small in met form. Prosthetic groups of these two components seemed, however, to be the same, protoporphyrin IX. The solubility in concentrated phosphate buffer (pH 6.6) of component F was far less than that of S, being least among those of Hb's of fishes so far tested6) (Fig. 4). Component F was much more heat-labile both in met and cyanmet form than S (Fig. 5). The heat stability of component F was comparable to that of mackerel Hb, the most labile Hb ever found for fish7), while component S was found to be one of the most stable Hb's7). Also regarding alkali resistance, component F was more labile than S (Fig. 6). Shape of the denaturation curve differed also between them, the curve of component F showing a sharp break in early phase of the reaction. Component F was electrophoretically homogeneous below pH 7.5, differing from component S which showed a single component over all the pH range covered (Fig. 7). From the pH vs. mobility curves (Fig. 8), the isoelectric points of components F and S are found to be pH's 5.7 and 7.8, respectively. The latter of such a high isoelectric point seems to be rare among Hb's of vertebrates 12). Column chromatographic behavior on CMC was also studied for both components. As pH of the developer (0.01 M phosphate buffer) was lowered, moving velocities of these components were decreased, at pH 6.5 that of component S being made almost to zero, while F not. Such a difference in chromatographic behavior may be applicable to quantitative separation of these two components.
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STUDIES ON MULTIPLE HEMOGLOBINS OF EEL-I:ABSORPTION SPECTRUM AND SOME OTHER PROPERTIES

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