Myosins were prepared from the ordinary muscle of 13 fish species such as skipjack, tuna, mackerel, and electrophoresed on SDS-polyacrylamide gradient gels. Resulting light chain regions were transferred to a GVHP membrane, and examined by immunoblotting technique for crossreactivity with the following anti-myosin light chain rabbit antisera: anti-skipjack Al, A2 and DTNB light chains, anti-round herring Al and anti-Alaska pollack Al antisera. Different blotting patterns were obtained depending on antiserum species used. Al and DTNB light chains generally showed a strong cross-reactivity, while A2 light chain did a rather weak reactivity. It was suggested from these results that myosin light chains have primary to higher-order structures in common throughout the three types of light chain and the fish species examined.
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