beta 2-Inhibin contains the active core of human seminal plasma beta-inhibin: synthesis and bioactivity.
The complete synthesis of the C-terminal 28 residues segment 67-94 of human seminal plasma beta-Inhibin, called beta 2-Inhibin, is reported. The Inhibin-like activity of the native 94 amino acids beta-Inhibin is compared to that of the synthetic replica of beta 2-Inhibin. In all assays used both peptides effectively suppress the FSH release induced by LHRH but have little effect on the LH release. In the mouse both peptides are equipotent on a mole basis. In the rat the synthetic beta 2-Inhibin is 3-10 times more potent than beta-Inhibin. Both peptides are active in rat anterior pituitary primary culture assays where maximum suppression of FSH release induced by LHRH occurs around 300 pmol/ml of beta 2-Inhibin. In contrast, maximum suppression of FSH release in the mouse pituitary assay occurs at 10-15 pmol/ml of either Inhibin.
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D005640:Follicle Stimulating Hormone / Q000378:metabolism; D007987:Gonadotropin-Releasing Hormone / Q000494:pharmacology; D006801:Humans; D007265:Inhibins; D007986:Luteinizing Hormone / Q000378:metabolism; D010446:Peptide Fragments; D010455:Peptides / Q000138:chemical synthesis* / Q000494:pharmacology; D010902:Pituitary Gland / Q000187:drug effects; D029584:Prostatic Secretory Proteins; D012661:Semen / Q000032:analysis*
D010446:Peptide Fragments; D010455:Peptides; D029584:Prostatic Secretory Proteins; C043076:beta-microseminoprotein; D007987:Gonadotropin-Releasing Hormone; D007265:Inhibins; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone; C044538:beta-inhibin (67-94)