Interrelationship between ovine follicular fluid inhibin and serum albumin.
Indian J Exp Biol
;
1992 Nov; 30(11): 1030-6
Article
in English
| IMSEAR
| ID: sea-59905
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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Protein Conformation
/
Peptide Mapping
/
Female
/
Serum Albumin
/
Sheep
/
Blotting, Western
/
Chromatography, Gel
/
Chromatography, Ion Exchange
/
Ovarian Follicle
/
Immune Sera
Language:
English
Journal:
Indian J Exp Biol
Year:
1992
Type:
Article
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