Purification of follitropin receptor from bovine calf testes.

作者: B Dattatreyamurty , S B Zhang , L E Reichert

DOI: 10.1016/S0021-9258(19)39389-5

关键词:

摘要: Follitropin (FSH) receptors were solubilized from pure light membranes of bovine calf testis, using an optimum detergent to protein ratio 0.01. The soluble FSH receptor fraction was gel filtered through Sepharose 6B isolate active (6B-Fr-1) which behaved as a complex and Gs protein. 6B-Fr-1 concentrated by ultrafiltration further purified sequential 4B filtration, DEAE-cellulose chromatography (to separate the protein), wheat germ lectin affinity chromatography. had FSH-binding capacity approximately 3.47 nmol/mg with Kd 1.9 X 10(-10) M. Yield 526 micrograms/11.5 kg tested. Radioiodinated, well unlabeled receptor, migrated on sodium dodecyl sulfate-polyacrylamide gels single major band Mr 240,000. This not affected 8 M urea treatment prior analysis electrophoresis, but dithiothreitol induced loss 240-kDa band, appearance 60,000 band. availability highly purified, stable should allow direct studies its structure-function relationships.

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