抄録
In starch gel electrophoresis of carp hemoglobin the patterns generally appeared obscurely, which was assumed to be caused by concomitant existence of metform, more or less, in the sample solutions of oxyhemoglobin. Therefore it was thought that the uniformity in the derivative form of hemoglobin was necessary for the experiment. For this purpose metform and also oxyform are unsuitable, the former trailing markedly and the latter being liable to autoxidation. As compared with those derivative forms, cyanmetform was found to be much more favorable, hemoglobin patterns in this form appearing clearly.
