Abstract

We have demonstrated the presence of MAP-2 in squirrel fish erythrophores using SDS-PAGE, immunoblot, and immunoprecipitation techniques. The monoclonal antibodies used (AP-9, -13, -14) were raised against distinct antigenic sites on Chinese hamster brain MAP-2. Immunoprecipitation studies demonstrated that all three antibodies bind a 300 K protein found in crude cell extracts and in partially purified MAP fractions isolated from erythrophores of the squirrel fish Holocentrus rufus. Immunofluorescent studies confirmed that the 300 K protein was present in cultured erythrophores. Studies of cells induced to aggregate and disperse their pigment granules revealed that the 300 K protein comigrated with the pigment, suggesting that the 300 K protein may constitute part of the "alpha-cytomatrix" involved in pigment translocations.

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