title: On multiple forms of bovine seminal plasma inhibin.
abstract: Out of a possible minimum of four, three distinct molecular species of bovine seminal plasma inhibin-differing either in Mr or in pI--have been purified to homogeneity. All three molecules exhibit the same proportion of alpha-helicity and beta-form when examined for their CD-spectra in a non-aqueous solvent medium. The implication of this finding for an induced conformation at the receptor-binding site for these hormonal peptides is briefly discussed.
authors.affiliation: Department of Zoology, University of Delhi.
authors.forename: A
authors.initials: A
authors.lastname: Sharma
authors.forename: P
authors.initials: P
authors.lastname: Malhotra
authors.forename: S
authors.initials: S
authors.lastname: Duraiswami
mesh_terms: D000818:Animals; D002417:Cattle; D007265:Inhibins / Q000737:chemistry / Q000302:isolation & purification*; D007526:Isoelectric Point; D008297:Male; D008970:Molecular Weight; D011487:Protein Conformation; D012661:Semen / Q000737:chemistry
chemical_list: D007265:Inhibins