HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Vonderhaar, B. K. Articles by Horn, T. M. Search for Related Content PubMed PubMed Citation Articles by Vonderhaar, B. K. Articles by Horn, T. M.

Isolation, Characterization, and Regulation of the Prolactin Receptor

Laboratory of Pathophysiology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20205

¹ To whom all reprints and correspondence should be addressed at National Institutes of Health, Bldg 10, Room 5B56, Bethesda, MD 20205 (301/496-3625).

ABSTRACT

The prolactin, or lactogenic hormone, receptor has been purified ( 80%) from lactating mouse liver and human term placenta by the nondenaturing zwitterionic detergent 3-[(3-cholamidopropyl) -dimethylammonio] -1-propane sulfonate and a prolactin affinity column. The isolated "core-binding unit" has a molecular weight of 37,000 ± 2,000 daltons. It retains the specificity for lactogenic hormones and binds prolactin with an affinity (K_a = 2 to 6 x 10⁹M^–1) similar to that of the receptor as it occurs in its membranous environment (K_a = 3 to 5 x 10⁹M^–1). Whether this "core-binding unit" exists on the cell surface in a cryptic or active form is influenced greatly by its association with other membrane proteins and the concentration of phosphatidylcholine within its local membranous environment.

² Tata Research, Development and Design Centre, 1 Mangaldas Road, Pune 411001 India.

³ Ospedale Maggiore Di San Giovanni Battista, E Delia Citta Di Torino, Institute Di Oncologia Di Torino, Via Cavour, 31-10123, Torino, Italy.