Binding of estrogen-3-sulfates to stallion plasma and equine serum albumin.
The binding of estrone-3-sulfate (E1-3-S) and estradiol-3-sulfate (E2-3-S) to adult stallion plasma was determined and compared with the binding to equine serum albumin (ESA). On the ESA molecule, two binding sites for E1-3-S with an association constant of 1.3 x 10(5) M-1 and several sites of weaker affinity were found; the data for E2-3-S showed the existence of four binding sites of moderate affinity (1 x 10(5) M-1) and several sites of weaker affinity. The removal of albumin from the stallion plasma resulted in the absence of binding of E1-3-S or E2-3-S, whereas the removal of glycoproteins resulted in binding parameters similar to those obtained with whole plasma. These results indicate that ESA is the only estrogen sulfate binder in horse plasma. Under physiological conditions, 95% of E1-3-S was bound to ESA.
Bouhamidi
R
R
Laboratoire de Biochimie, CNRS URA 609, Université, Caen, France.
Gaillard
J L
JL
Silberzahn
P
P
Martin
B
B
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism; D004958:Estradiol / Q000031:analogs & derivatives* / Q000378:metabolism; D004970:Estrone / Q000031:analogs & derivatives* / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D006736:Horses / Q000097:blood*; D008297:Male; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*
D001798:Blood Proteins; D006023:Glycoproteins; D012709:Serum Albumin; D004970:Estrone; C028628:estradiol-3-sulfate; D004958:Estradiol; C017296:estrone sulfate