PMID: 36884Mar 15, 1979

Characterization of prolactin binding by membrane preparations from rat liver

The Biochemical Journal
A M Silverstein, J F Richards

Abstract

Binding sites for prolactin were identified in a plasma-membrane-enriched fraction isolated from livers of mature female rats. 125I-labelled sheep prolactin prepared by the lactoperoxidase procedure retained the same molecular integrity and binding affinity as the native hormone at physiological pH. The receptors bound prolactin from different species, whereas non-lactogenic hormones were not bound. The binding of 125I-labelled sheep prolactin was activated equally by bivalent and univalent cations, bivalent cations exerting their maximal effect at much lower concentrations. The association of 125I-labelled sheep prolactin with the receptor was a time- and temperature-dependent process. Partial dissociation was detected. The binding of 125I-labelled sheep prolactin was strongly influenced by pH, with an optimum observed at pH 6.5. Receptor activity was destroyed by Pronase and phospholipase C, whereas neuraminidase increased binding. Treatment of the membranes by ribonuclease and deoxyribonuclease did not affect the binding. Binding of 125I-labelled sheep prolactin was inhibited by p-chloromercuribenzoic acid, dithiothreitol and by brief exposure to high temperatures. Scatchard analysis of the binding of 125I-labelled sheep pro...Continue Reading

References

Mar 1, 1988·Brain, Behavior, and Immunity·L MateraE Genazzani
Mar 1, 1988·General and Comparative Endocrinology·G MuccioliR Di Carlo
Sep 1, 1981·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·W H Evans
May 1, 1984·International Journal of Peptide and Protein Research·C H ChengR C Pak

Related Concepts

Exertion
Tissue Membrane
Dnase1
Mammary Gland
Hormone Receptors, Cell Surface
Dithiothreitol
Neuraminidase
Neu1
Cations
Lactoperoxidase

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