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Abstract
Myosin from carp white muscle contains two mol of "DTNB" light chain (mol. wt 17 500 daltons) and two mol of "alkali" light chains (mol. wt 25 000 and 16 400 daltons). The three light chains have been isolated in pure state and characterized by electrofocusing, ultraviolet absorption, amino acid analysis and tryptic peptide mapping. Our results show a great homology between the two carp alkali light chains whereas LC2 seems chemically more different. But the homology of LC1 and LC3 is not so extensive as in the case of the higher vertebrate myosin.
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