Abstract
The precursor to a seminal plasma protein reported to have inhibin-like activity was characterized through cDNA cloning and sequencing. It is a 114-amino-acid polypeptide which differs from its seminal plasma derivative mainly by the presence of a 20-residue amino-terminal extension, a putative signal sequence, carrying a possible N-glycosylation site. The protein is specified by a single gene per haploid genome. Its mRNA is detectable in the prostate but not in the testis, which suggests that it is primarily a prostatic secretory protein.
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