FEBS Letters · 1984 · 112 citations · 21 references
Life SciencesBiochemistryEndocrinologyReproductive BiologyReproductive EndocrinologyReproductive PhysiologyPlasma ProteinsProteolytic EnzymesProteolytic ProcessingInhibin RegulationInhibin SecretionSeminal Plasma BiochemistrySeminal Plasma CompositionSeminal Plasma Modulation
The complete sequence of a 94 amino acid human seminal plasma polypeptide exhibiting inhibin-like activity is presented. This molecule, called beta-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 Gln-Arg cleavage to release the basic C-terminal active moiety.
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N‐terminally extended somatostatin: The primary structure of somatostatin‐28
Lucien Pradayrol, Hans Jörnvall, Viktor Mutt et al. · FEBS Letters · 1980 · 529 citations · Full text
Dual Endocrine Activity of the Testes
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