On multiple forms of bovine seminal plasma inhibin.
Indian J Biochem Biophys
;
1991 Oct-Dec; 28(5-6): 485-90
Article
Dans Anglais
| IMSEAR
| ID: sea-27995
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.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Conformation des protéines
/
Sperme
/
Mâle
/
Bovins
/
Inhibines
/
Point isoélectrique
/
Animaux
/
Masse moléculaire
langue:
Anglais
Texte intégral:
Indian J Biochem Biophys
Année:
1991
Type:
Article
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