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The high molecular weight microtubule-associated proteins (MAPs) consist of MAPs 1A, 1B, 1C, 2A, and 2B. The proteins have been prepared from rat brain by using taxol and resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The individual proteins were purified by electro-elution from stained fixed gels and shown to migrate at their original mobility without proteolysis. Amino acid compositions of purified MAP 1 and 2 component proteins are reported and compared.
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