β2‐Inhibin contains the active core of human seminal plasma β‐inhibin: synthesis and bioactivity

摘要

>The complete synthesis of the C-terminal 28 residues segment 67–94 of human seminal plasma jS-Inhibin, called β₂-Inhibin, is reported. The Inhibin-like activity of the native 94 amino acids β-Inhibin is compared to that of the synthetic replica of β₂-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 β₂-Inhibin is 3–10 times more potent than β-Inhibin. Both peptides are active in rat anterior pituitary primary culture assays where maximum suppression of FSH release induced by LHRH occurs around 300 data-equation-construct="true" class="math-equation-construct"> data-equation-image="true" class="math-equation-image"> alt="math formula" src="http://onlinelibrary.wiley.com/store/10.1016/0014-5793(85)81113-3/asset/equation/feb20014579385811133-math-si1.gif?v=1&s=df2dc911a8ce92e4e5365282121dee9256ef224f" class="inlineGraphic" /> data-equation-mathml="true" class="math-equation-mathml" style="display:none"> of β₂-Inhibin. In contrast, maximum suppression of FSH release in the mouse pituitary assay occurs at 10–15 data-equation-construct="true" class="math-equation-construct"> data-equation-image="true" class="math-equation-image"> alt="math formula" src="http://onlinelibrary.wiley.com/store/10.1016/0014-5793(85)81113-3/asset/equation/feb20014579385811133-math-si2.gif?v=1&s=a7cfda01347ce8937eb0a2df256b86e29c6d5006" class="inlineGraphic" /> data-equation-mathml="true" class="math-equation-mathml" style="display:none"> of either Inhibin.