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Journal of Clinical Endocrinology & Metabolism Vol. 68, No. 5 938-945
doi:10.1210/jcem-68-5-938
Copyright © 1989 by the Endocrine Society.
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Human Serum Does Not Contain a High Affinity Estrogen-Binding Glycoprotein Different from Sex Hormone-Binding Globulin*

JEAN-LUC RENY and ANA M. SOTO

Department of Anatomy and Cellular Biology, Tufts University School of Medicine Boston, Massachusetts 02111

Address all correspondence and requests for reprints to: Dr. Ana M. Soto, Department of Anatomy and Cellular Biology, Tufts University, 136 Harrison Avenue, 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 estradiolbinding protein of serum is most likely SHBG.

* This work was supported by NIH Grant CA-13410 and EPA Grant CR-813481-01.

Received September 7, 1988.






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Copyright © 1989 by The Endocrine Society