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  E-mail Message: I thought you might be interested in this item at http://www.worldcat.org/oclc/114168321 Title: Hepatic progesterone receptors: characterization in the turtle Chrysemys picta. Publisher: ISBN/ISSN: 0013-7227 OCLC:114168321

  
  

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Hepatic progesterone receptors: characterization in the turtle Chrysemys picta.

Author:	D Riley; JC Reese; IP Callard
Edition/Format:	Article : English
Publication:	Endocrinology, 1988 Aug; 123(2): 1195-201
Database:	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Summary:	High and low affinity progesterone (P)-binding proteins similar to those described in the chick oviduct were characterized for the first time in liver cytosol in an oviparous turtle, Chrysemys picta. Two forms of high affinity P receptor were separated by diethyl aminoethyl (DEAE)-Sepharose anion exchange chromatography; the A form eluted in low salt buffer, and the B form at a KCl concentration of 0.20 M in a linear gradient. After photoaffinity labeling of crude cytosol with [3H] R5020, two overlapping peaks of radioactivity were detected with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. After separation with DEAE-Sepharose and photoaffinity labeling, the A form migrated as a single peak with a mol wt of 90,000, and the B form as a single peak with a mol wt of 123,000. The affinity (Kd, 2.9 X 10(-9) M), capacity (1 pmol/mg protein), and binding specificity were characteristic of a P receptor. P competed most effectively for [3H]P binding. R5020 and deoxycorticosterone were good competitors; 5 alpha-pregnenolone, 17 alpha-hydroxyprogesterone, and testosterone were quite effective; cortisol, corticosterone, aldosterone, and 5 alpha-dihydrotestosterone were poor competitors. A lower affinity P-binding component (Kd, 1 X 10(-7) M; maximum binding, 15 pmol/mg protein) co-eluted from DEAE-Sepharose columns with the A and B receptor forms. This is the first description of a hepatic P receptor in any vertebrate.  Read more...
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