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Journal of Clinical Endocrinology & Metabolism, Vol 68, 938-945, Copyright © 1989 by Endocrine Society

ARTICLES

Human serum does not contain a high affinity estrogen-binding glycoprotein different from sex hormone-binding globulin

JL Reny and AM Soto
Department of Anatomy and Cellular Biology, Tufts University School of Medicine, Boston, Massachusetts 02111.

The mannoglycoprotein fraction obtained by Concanavalin-A chromatography of human serum binds both androgens and estrogens with high affinity. Sex hormone-binding globulin (SHBG) is a component of this fraction that binds both steroids, but the fraction may contain another component that binds only estrogen. We used several chromatographic methods to ascertain whether the estradiol-binding properties of the mannoglycoprotein fraction could be attributed to SHBG or to SHBG and the putative estrogen-binding protein. DEAE- trisacryl, chromatofocusing, and anti-SHBG-immunoglobulin Sepharose chromatography resulted in coelution of the androgen- and estrogen- binding activities. SHBG purified by ligand affinity chromatography as well as immunoaffinity-purified SHBG had estradiol-binding properties similar to those of the crude mannoglycoprotein preparation. These data strongly suggest that 1) SHBG is the only estradiol-binding protein in the mannoglycoprotein fraction obtained by Concanavalin-A chromatography of human serum, and 2) the putative estradiol-binding protein of serum is most likely SHBG.




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Copyright © 1989 by The Endocrine Society