期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1982
卷号：79
期号：19
页码：5930-5934
DOI：10.1073/pnas.79.19.5930
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A prolactin receptor was purified from a solubilized preparation of mouse microsomal membranes by affinity chromatography. The receptors were solubilized with the detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate)(Chaps) a zwitterionic derivative of cholic acid. The affinity gel was prepared by coupling ovine prolactin to CH-Sepharose 4B. After extensive elution of the nonspecifically adsorbed proteins, the receptors were eluted with 4 M urea/1 M NaCl/0.5% Chaps followed by 5 M MgCl2/0.5% Chaps. The eluted receptor appeared on NaDodSO4/polyacrylamide gels as a single major band of Mr 37,000. The purified receptor retained its specificity for lactogenic hormones and binds 125I-labeled ovine prolactin with a Ka of 2-6 X 10(9) M-1.
