Abstract

The immunological relation between 14S dynein and 30S dynein obtained from Tetrahymena cilia was investigated by using antisera specific for each dynein subunit or some dynein subunits separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Although 14 and 30S dynein main subunits have different electrophoretic mobilities, our immunodiffusion tests showed that there exists a close immunological relation between them. At least three immunologically different polypeptides designated polypeptides A, B and C are included in the 30S dynein main band which has been recognized as a single component by electrophoresis, and that the polypeptides designated A', B', and C' are included in the 14S dynein main bands. Polypeptides A and A', B and B', or C and C' appeared to have a certain common antigenic determinant(s). Polypeptide C of 30S dynein was shown to possess a certain antigenic determinant(s) specific for 30S dynein, besides the determinant common with that of polypeptide C' of 14S dynein. The second main component of 30S dynein proved to be a specific polypeptide of 30S dynein but not to be a degraded product of the main polypeptide. All antisera reacted with native dynein molecules to some extent, but did not inhibit dynein ATPase (ATP phosphohydrase, EC 3.6.1.3) activity significantly.

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