AbstractThe complete sequence of a 94 amino acid human seminal plasma polypeptide exhibiting inhibin-like activity is presented. This molecule, called β-inhibin, selectively and specifically suppresses the release of pituitary FSH in vivo as well as in vitro. It does not affect the secretion of LH. Such a novel acidic protein contains a very basic C-terminal segment which is easily cleaved by mild tryptic digestion. It is predicted that the FSH inhibiting activity may reside within this region of the molecule. This would imply a post Gin-Arg cleavage to release the basic C-terminal active moiety
AbstractThe predominant basic protein in liquefied human seminal plasma is the major degradation pro...
AbstractA 94-residue polypeptide isolated from human seminal plasma and its chemically synthesized C...
Observation of contradictory results with the in vitro assays for inhibin-like activity of the carbo...
AbstractThe complete sequence of a 94 amino acid human seminal plasma polypeptide exhibiting inhibin...
The complete sequence of a 94 amino acid human seminal plasma polypeptide exhibiting inhibin-like ac...
AbstractAn extract of human seminal plasma was found to have inhibin-like activity. The active facto...
AbstractA polypeptide in preparations of ‘large’ form (Mr ∼14 000) material with inhibin-like activi...
AbstractThe complete synthesis of the C-terminal 28 residues segment 67–94 of human seminal plasma j...
Human seminal plasma contains a factor(s) which preferentially suppress the release of FSH from the ...
AbstractThe complete synthesis of the C-terminal 28 residues segment 67–94 of human seminal plasma j...
AbstractThe amino acid sequence of a large form of inhibin-like peptide in human seminal plasma was ...
AbstractAn extract of human seminal plasma was found to have inhibin-like activity. The active facto...
A polypeptide in preparations of 'large' form (M<SUB>r</SUB> ~ 14000) material with inhibin-like act...
AbstractA polypeptide in preparations of ‘large’ form (Mr ∼14 000) material with inhibin-like activi...
Two moieties of inhibin could be obtained by chromatography of partially purified preparations of in...
AbstractThe predominant basic protein in liquefied human seminal plasma is the major degradation pro...
AbstractA 94-residue polypeptide isolated from human seminal plasma and its chemically synthesized C...
Observation of contradictory results with the in vitro assays for inhibin-like activity of the carbo...
AbstractThe complete sequence of a 94 amino acid human seminal plasma polypeptide exhibiting inhibin...
The complete sequence of a 94 amino acid human seminal plasma polypeptide exhibiting inhibin-like ac...
AbstractAn extract of human seminal plasma was found to have inhibin-like activity. The active facto...
AbstractA polypeptide in preparations of ‘large’ form (Mr ∼14 000) material with inhibin-like activi...
AbstractThe complete synthesis of the C-terminal 28 residues segment 67–94 of human seminal plasma j...
Human seminal plasma contains a factor(s) which preferentially suppress the release of FSH from the ...
AbstractThe complete synthesis of the C-terminal 28 residues segment 67–94 of human seminal plasma j...
AbstractThe amino acid sequence of a large form of inhibin-like peptide in human seminal plasma was ...
AbstractAn extract of human seminal plasma was found to have inhibin-like activity. The active facto...
A polypeptide in preparations of 'large' form (M<SUB>r</SUB> ~ 14000) material with inhibin-like act...
AbstractA polypeptide in preparations of ‘large’ form (Mr ∼14 000) material with inhibin-like activi...
Two moieties of inhibin could be obtained by chromatography of partially purified preparations of in...
AbstractThe predominant basic protein in liquefied human seminal plasma is the major degradation pro...
AbstractA 94-residue polypeptide isolated from human seminal plasma and its chemically synthesized C...
Observation of contradictory results with the in vitro assays for inhibin-like activity of the carbo...