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Characterization of a testis specific antigen in the mouse
The partial characterization of a mouse hydrosoluble testis specific protein by crossed immunoelectrophoresis, ion-exchange chromatography and SDS-Page was made. This protein presented a low electrophoretic motility at pH 8.6. It was not adsorbed to DEAE-Sephacel at pH 8.6, but was slightly adsorbed at pH 9.0, while in CM-Sephadex it was readily adsorbed at pH 6.0, indicating the basic nature of this protein. The apparent molecular weight was determined to be of 28 Kd by SDS-Page. The previously reported testis specificity of this protein was corroborated by its absence in a liver extract.
The partial characterization of a mouse hydrosoluble testis specific protein by crossed immunoelectrophoresis, ion-exchange chromatography and SDS-Page was made. This protein presented a low electrophoretic motility at pH 8.6. It was not adsorbed to DEAE-Sephacel at pH 8.6, but was slightly adsorbed at pH 9.0, while in CM-Sephadex it was readily adsorbed at pH 6.0, indicating the basic nature of this protein. The apparent molecular weight was determined to be of 28 Kd by SDS-Page. The previously reported testis specificity of this protein was corroborated by its absence in a liver extract.