Isolation, Characterization, and Regulation of the Prolactin Receptor
Open Access
- 1 February 1985
- journal article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 68 (2) , 466-488
- https://doi.org/10.3168/jds.s0022-0302(85)80847-x
Abstract
The prolactin, or lactogenic hormone, receptor has been purified (approximately 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 (Ka = 2 to 6 X 10(9) M-1) similar to that of the receptor as it occurs in its membranous environment (Ka = 3 to 5 X 10(9) M-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.Keywords
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