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Department of Biological Science, Florida State University Tallahassee, Florida 32306
Abstract
A protein that suppresses GnRH-stimulated LH release from dispersed rat anterior pituitary cells was purified from rat hypothalami by chromatography on Sephadex G-25, carboxymethyl cellulose, and high performance gel permeation. The final increase in inhibitory activity was 214-fold. The inhibitor is a glycoprotein with an apparent mol wt of 12,252 ± 638, as determined by gel permeation on HPLC and electrophoreses as a monomer after treatment with 8 M urea. The inhibitor has a Stokes radius of 16 A, an S value of 2.14 ± 0.08, an isoelectric point value near 4.1, and a frictional ratio of 1.05. A preliminary amino acid composition is presented. (Endocrinology 120: 483–490,1987)
Footnotes
* This work was supported by NSF Grant PCM-8120408 and the Ford and Mellon II Foundations.
To whom all correspondence and requests for reprints should be addressed.
Received December 26, 1985.
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