Homogenous a and p subunits were isolated for the first time in preparative amounts in the presence of sodium dodecyl sulfate. Analysis by analytical polyacrylamide electrophoresis, sedimentation velocity, and immunoprecipitation with monospecific antibodies indicated homogeneity. The apparent molecular masses of the purified subunits as determined electrophoretically in the presence of dodecyl sulfate are: a = 140.2 A 2.1 kDa and p = 123 1.8 kDa. Amino acid analyses show that per 100 mol amino acid the a-subunit has a higher serine content (Ser,/Sers = 1.32, Ser,/Ser, = 1.42) and a lower aspartic acid/asparagine (Asx) content (Asx,/Asxp =

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