Cross-referencing testis-specific nuclear proteins by two-dimensional gel electrophoresis.

Discontinuous sodium sodecyl sulfate-gel electrophoresis combined with acid-urea gel electrophoresis reveals that both testis histone H1 classes TH1-X (Branson, R. E., Grimes, S. R., Jr., Yonuschot, G., and Irvin, J. L (1975) Arch. Biochem. Biophys. 168, 403-412) and H1 contain two polypeptides each. Migration properties and relative staining intensities of the four H1 histone proteins in testis support the following conclusions. 1. Two testis-specific forms become the major H1 components at some stage of spermatogenesis. 2. During this stage they assume structural and functional role analogous to those of their two somatic counterparts. We have also detected a new testis-specific protein containing cysteine.