Reference : Purification and characterization of a bovine pregnancy-associated glycoprotein
Scientific journals : Article
Life sciences : Veterinary medicine & animal health
http://hdl.handle.net/2268/5813
Purification and characterization of a bovine pregnancy-associated glycoprotein
English
[fr] Purification et caractérisation d'une protéine associée à la gestation
Zoli, André Pagnah [Université de Liège - ULG > Faculté de Médecine Vétérinaire > > >]
Beckers, Jean-François mailto [Université de Liège - ULg > Département de sciences fonctionnelles > Physiologie de la reproduction >]
Wouters-Ballman, Patricia [Université de Liège - ULG > Faculté de Médecine Vétérinaire > > >]
Closset, Jean [Université de Liège - ULg > > Biochimie générale, humaine et pathologique > > >]
Falmagne, Paul [Université de Mons-Hainaut - UMH > Faculté des Sciences > Chimie biologique > >]
Ectors, Francis [Université de Liège - ULg > Services généraux (Faculté de médecine vétérinaire) > Relations académiques et scientifiques (Méd. vétérinaire) >]
Jul-1991
Biology of Reproduction
Society for the Study of Reproduction
45
1
1-10
Yes (verified by ORBi)
International
0006-3363
1529-7268
Madison
WI
[en] Purification ; Characterization ; PAG
[fr] Purification ; Charactérisation ; PAG
[en] A 67000 Mr bovine pregnancy-associated glycoprotein (bPAG) has been isolated from fetal cotyledons and purified to homogeneity by HPLC. The purification was monitored by a double immunodiffusion test and by RIA in conjunction with an antiserum raised against a crude fraction of placenta-specific antigens. The molecular weight of bPAG was estimated to be 67000 by SDS-PAGE. The isoelectric points (pI) of the four isoforms, determined by high-resolution analytical electrofocusing in polyacrylamide gel, were 4.4, 4.6, 5.2, and 5.4. The carbohydrate content of the bPAG consisted of approximately 10.02 +/- 1.09% neutral sugar and variant amounts of sialic acid (from 0.29 +/- 0.06% in the most basic isoform to 2.1 +/- 0.31% in the most acidic isoform). A specific antiserum was raised against the purified bPAG. A specific RIA showed that the bPAG was antigenically unrelated to BSA, alphafetoprotein (AFP), and human schwangerschafts-spezifischen (pregnancy-specific) beta 1 glycoprotein (SP1). According to some characteristics (e.g. the molecular weight), the purified bPAG may correspond to a form of the pregnancy-specific protein B previously described by Sasser and colleagues (Biol Reprod 1986; 35:936-942).
Laboratoire d'Endocrinologie et de Physiologie de la Reproduction animale
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/5813

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