125I-Labelled thyrotrophin (TSH) showed saturable binding to hyperplastic guinea-pig thyroid slices in vitro, but not to kidney, adrenal, liver, testis or salivary gland slices. Two populations of binding sites were demonstrated: high order sites showed an affinity constant of 3·8 × 1081/mol and a capacity of 8 × 103 molecules of TSH/cell; low order sites, affinity constant of 2·9 × 1071/mol and capacity of 8 × 104 molecules/cell. The highorder sites saturate at about 1 mu./ml, approximately the level producing maximal in-vivo and in-vitro responses. Binding of 125I-labelled TSH was reversible, the released hormone appearing substantially unchanged as assessed by chromatographic behaviour and antiserum binding. Release of unlabelled TSH from pre-incubated thyroid slices was demonstrated by bioassay. Bovine thyroid slices were found to have a lower capacity for binding than hyperplastic guinea-pig slices.
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