HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by MANLEY, S. W. Articles by HAWKER, R. W. Search for Related Content PubMed PubMed Citation Articles by MANLEY, S. W. Articles by HAWKER, R. W.

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 x 10⁸1/mol and a capacity of 8 x 10³ molecules of TSH/cell; low order sites, affinity constant of 2·9 x 10⁷1/mol and capacity of 8 x 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.

This article has been cited by other articles:

				B. Rapoport, G. D. Chazenbalk, J. C. Jaume, and S. M. McLachlan The Thyrotropin (TSH)-Releasing Hormone Receptor: Interaction with TSH and Autoantibodies Endocr. Rev., December 1, 1998; 19(6): 673 - 716. [Abstract] [Full Text]