Abstract
125I-human chorionic gonadotropin (125I-hCG) bound to plasma membranes of bovine corpora lutea consisted of reversible and not readily reversible fractions. The not readily reversible fraction progressively increased as the length and the temperature of preincubation were increased. The not readily reversible fraction was, however, completely eluted after any time or temperature of preincubation. Although the not readily reversible and reversible bound 125I-hCG were precipitated equally well with 10% trichloroacetic acid, the not readily reversible bound 125I-hCG was able to rebind much higher to fresh plasma membranes compared to reversible bound 125I-hCG. These findings suggest that while not readily reversible bound 125I-hCG was intact, the reversible bound 125I-hCG was somewhat altered during the binding reaction.
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Rao, C.V., Carman, F.R. The nature of reversible and not readily reversible bovine corpus luteum plasma membranes bound human chorionic gonadotropin. J Endocrinol Invest 9, 403–406 (1986). https://doi.org/10.1007/BF03346951
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DOI: https://doi.org/10.1007/BF03346951