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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Jun;78(6):3973–3975. doi: 10.1073/pnas.78.6.3973

Characterization of specific receptors for calcitonin in porcine lung.

M Fouchereau-Peron, M S Moukhtar, A A Benson, G Milhaud
PMCID: PMC319696  PMID: 6267614

Abstract

The binding of salmon calcitonin was investigated in subcellular fractions obtained from normal porcine lung. Only the membrane fraction (density, 1.14 g/cm3) showed specific binding for calcitonin. Specific binding of 125I-labeled salmon calcitonin was competitively inhibited by concentrations of unlabeled homologous hormone in the range 0.01-1 nM. Half-maximal inhibition of binding was observed with 0.12 nM salmon calcitonin. Scatchard analysis of the data suggested the presence of one class of binding sites with a mean affinity constant of 0.9 X 10(10) M-1 and a mean receptor number of 40 X 10(8)/mg of protein. The binding of salmon calcitonin was highly specific; half-maximal inhibition of binding was observed with 63.8 nM bovine calcitonin, the hormone corticotropin having no effect in this system.

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Selected References

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