title: Interrelationship between ovine follicular fluid inhibin and serum albumin.
abstract: Ovine follicular fluid inhibin (oFF-I) as isolated in this laboratory, proved to be a monomeric protein (M(r).65 kDa). It was found to share very many of the physico-chemical characteristics of ovine serum albumin (oSA)-such as molecular size, iso-electric point, N-terminal aminoacid, finger-print patterns following enzymatic or cyanogen bromide cleavage, as well as binding of estradiol-17 beta and tryptophan. Furthermore, an antiserum containing polyclonal antibodies to oSA showed perfect cross-reaction with oFF-I. Nevertheless, oFF-I is distinct and different from oSA, as would be evident from the data reported here. Of the two proteins, oFF-I alone is capable of suppressing pituitary FSH output in a dose-dependent manner. Secondly, an antiserum containing polyclonal antibodies against Fraction-S2, a partially purified, biologically active fragment (M(r): 30-40 kDa)-derived from oFF-I, cross-reacted with the 65 kDa inhibin, but did not recognize oSA. Finally, the CD-spectra of the two proteins, when examined as a function of pH, show characteristic differences.
authors.affiliation: Department of Zoology, University of Delhi, India.
authors.forename: N
authors.initials: N
authors.lastname: Kumar
authors.forename: S
authors.initials: S
authors.lastname: Gupta
authors.forename: S
authors.initials: S
authors.lastname: Duraiswami
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005260:Female; D007106:Immune Sera; D007265:Inhibins / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification; D008970:Molecular Weight; D006080:Ovarian Follicle / Q000502:physiology; D010449:Peptide Mapping; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry* / Q000276:immunology; D012756:Sheep
chemical_list: D007106:Immune Sera; D012709:Serum Albumin; D007265:Inhibins