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  • Title: Isolation, characterization, and regulation of the prolactin receptor.
    Author: Vonderhaar BK, Bhattacharya A, Alhadi T, Liscia DS, Andrew EM, Young JK, Ginsburg E, Bhattacharjee M, Horn TM.
    Journal: J Dairy Sci; 1985 Feb; 68(2):466-88. PubMed ID: 2985666.
    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.
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