A polypeptide in preparations of ‘large’ form (M
r ∼14 000) material with inhibin‐like activity (inhibiting FSH secretion) has been isolated from human seminal plasma. Its amino acid composition, cleavage pattern with CNBr, N‐terminal sequence, and properties on reverse‐phase high‐performance liquid chromatography establish this inhibin‐like preparation to be homogeneous. The polypeptide contains close to 130 residues, has a free N‐terminal serine residue, a methionine residue in position 19, and a dibasic structure (Arg—Lys) in positions 16–17.
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