Studies on the proteins of fish skeletal muscle. 1. Electrophoretic analysis of codling extracts of low ionic strength

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Abstract
Extracts of codling (Gadus callarius) skeletal muscle at 0.05, 0.1 and 0.2 I, pH 7.5, were examined in the Tiselius electrophoresis apparatus. Extracts at 0.05 I, pH 7.5, proved to be the most informative, and revealed the presence of at least 7 components which may be divided into Jacob''s groups I, H and III. Whereas groups II and III of codling bear similarities to the corresponding groups of rabbit, group I is quite different. Group II appears to be particularly significant in relation to the denaturation of these protein mixtures. The mobilities of codling muscle proteins are appreciably greater than those of rabbit. The influence of ionic strength on the mobilities of these proteins was examined. On dialysis of a 0.05 I extract against distilled water, component 2 precipitates completely, and all the components, except perhaps 5, suffer a partial loss of solubility. The precipitate of globulin X is only partially re-soluble; the soluble portion shows 3 main components which on the basis of mobility can be related to components in the original extract. However, estimates of composition reveal that the relationship is complex.