A basic protein with a relative molecular mass of 19 kDa has been identified and isolated to purity from sonication-resistant, partially demembranized human sperm nuclei. Several criteria prove that this is the unique sperm-specific protein, which was previously thought to be a sperm/testis histone. Partial primary structure sequencing demonstrates homologies with human seminal alpha-inhibins and semenogelin. From the sequence and Western-blotting data with antibodies against basic seminal inhibin-like peptide, we propose that this 19-kD protein is a product of 52-kDa semenogelin processing. The 19-kDa protein was not found among seminal plasma proteins and may be protected from further cleavage into inhibin-like peptides by its association with the sperm head. Immunofluorescence data indicate its localization in the nuclear periphery, with preferential concentration at the acrosome calyx boundary.
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Zalensky et al. (1993) studied this question.
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