Analyze Diet
The Journal of steroid biochemistry and molecular biology1992; 42(3-4); 345-349; doi: 10.1016/0960-0760(92)90138-9

Binding of estrogen-3-sulfates to stallion plasma and equine serum albumin.

Abstract: 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.
Publication Date: 1992-05-01 PubMed ID: 1606045DOI: 10.1016/0960-0760(92)90138-9Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article discusses the binding of two types of estrogen sulfates (estrone-3-sulfate and estradiol-3-sulfate) to adult stallion plasma and equine serum albumin, a type of protein found in horses. It was determined that equine serum albumin is the only effective binding agent for these estrogen sulfates in horse plasma.

Understanding the Binding of Estrogen-3-Sulfates

  • The research conducted aimed to understand how estrone-3-sulfate (E1-3-S) and estradiol-3-sulfate (E2-3-S) bind to adult stallion plasma and equine serum albumin (ESA).
  • These two substances are types of estrogen sulfates, a group of steroids hormones that play important roles in the reproductive functioning of horses.

Findings on the Equine Serum Albumin Molecule

  • On the ESA molecule, the researchers found two binding sites for E1-3-S. These sites had an association constant of 1.3 x 10(5) M-1, indicating a high level of binding affinity.
  • On top of these two high-affinity sites, several additional sites of weaker binding affinity were found.
  • For E2-3-S, there were four sites of moderate affinity (1 x 10(5) M-1) found, along with several weaker sites.

Effect of Albumin Removal

  • When the researchers removed albumin from the stallion plasma, they observed no binding of E1-3-S or E2-3-S.
  • However, when they removed glycoproteins from the plasma, the binding parameters remained similar to those of the whole plasma, indicating the importance of ESA for the binding process.

Conclusions on ESA’s Role

  • All these results pointed towards the conclusion that ESA is the single binder for estrogen sulfate in horse plasma.
  • Under physiological conditions, approximately 95% of E1-3-S was found to be bound to ESA, signalling the significant role of this protein in managing these hormones within the horse body.

Cite This Article

APA
Bouhamidi R, Gaillard JL, Silberzahn P, Martin B. (1992). Binding of estrogen-3-sulfates to stallion plasma and equine serum albumin. J Steroid Biochem Mol Biol, 42(3-4), 345-349. https://doi.org/10.1016/0960-0760(92)90138-9

Publication

ISSN: 0960-0760
NlmUniqueID: 9015483
Country: England
Language: English
Volume: 42
Issue: 3-4
Pages: 345-349

Researcher Affiliations

Bouhamidi, R
  • Laboratoire de Biochimie, CNRS URA 609, Université, Caen, France.
Gaillard, J L
    Silberzahn, P
      Martin, B

        MeSH Terms

        • Animals
        • Blood Proteins / metabolism
        • Estradiol / analogs & derivatives
        • Estradiol / metabolism
        • Estrone / analogs & derivatives
        • Estrone / metabolism
        • Glycoproteins / metabolism
        • Horses / blood
        • Male
        • Protein Binding
        • Serum Albumin / metabolism

        Citations

        This article has been cited 2 times.
        1. Bone C, Squires EJ. The Binding of Free and Sulfated Androstenone in the Plasma of the Boar. Animals (Basel) 2021 May 20;11(5).
          doi: 10.3390/ani11051464pubmed: 34065189google scholar: lookup
        2. Vanwert AL, Bailey RM, Sweet DH. Organic anion transporter 3 (Oat3/Slc22a8) knockout mice exhibit altered clearance and distribution of penicillin G. Am J Physiol Renal Physiol 2007 Oct;293(4):F1332-41.
          doi: 10.1152/ajprenal.00319.2007pubmed: 17686950google scholar: lookup