Carp myogens of white and red muscles. General composition and isolation of low-molecular-weight components of abnormal amino acid composition

1. The general composition of the carp myogens of white and red muscles was examined by electrophoresis and ultracentrifugation. 2. Eight and nine peaks were found in the electrophoretic analysis at pH7·3 and I0·075 of white and red muscle respectively. Lowering of the pH to 5 or 6 did not increase the number of peaks. The electrophoretic pattern of white-muscle myogen was remarkably different from that of red-muscle myogen, though ultracentrifugal analyses of the both types of myogen gave similar diagrams, in which about one-third of the total myogen sedimented slowly. 3. The pH–mobility curves of the myogen of white muscle indicated that the net charges of the components 2, 3 and 5 vary only slightly within the pH range 7·3–5·4, suggesting that their histidine content is very low. 4. The slow-sedimenting fraction of white-muscle myogen was isolated in fairly good yield by ammonium sulphate fractionation, by taking advantage of their high salting-out range, and the fraction was shown to be composed mainly of components 2, 3 and 5. 5. The same method of fractionation was applied to red-muscle myogen and the absence of the three components was confirmed. These results bring to light a new difference between the two types of fish muscle.