Abstract
Plasma membranes from bovine corpora lutea have been purified by sucrose density gradient centrifugation. The purified membranes, in addition to binding 125I-hCG, also possess hCG-stimulated adenylate cyclase and NaK-ATPase. The relative purification of 125I-hCG binding, adenylate cyclase and NaK-ATPase on the basis of the specific activities in the whole homogenate were 7.8, 6.4 and 2.6, respectively. The presence of both the hormone sensitive adenylate cyclase and 125I-hCG binding activities suggest that these plasma membranes might possess the ‘receptor’ for gonadotropin.
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