A murine monoclonal antibody derived from the immunization of human thyroglobulin reacts equally with L-thyroxine and reverse triiodo-L-thyronine and has a unique idiotype.
- 1 January 1986
- journal article
- research article
- Published by Japan Endocrine Society in Endocrinologia Japonica
- Vol. 33 (5) , 629-636
- https://doi.org/10.1507/endocrj1954.33.629
Abstract
Murine monoclonal antibody (mAb 16.3.2) to human thyroglobulin whichbound equally to various thyroglobulins derived from nine species was oqtainedfrom the fusion of C3H/He spleen cells sensitized with normal human thyroglobulin.Characterization of mAb 16.3.2 revealed that both L-thyroxine (T4) and reverse triiodo-L-thyorine (rT3) were very efficient in the competitivebinding inhibition test and that a molar ratio between T4 and rT3 needed for 50% inhibition of binding to immunized thyroglobulin was about 1: 1.Further studies on the idiotype of mAb 16.3.2 using both binding and competitivebinding inhibition tests showed that mAb 16.3.2 had a unique idiotypenot cross-reacting with other monoclonal antibodies to thyroglobulins.Therefore, a possible explanation offered was that mAb 16.3.2 was endowed with aunique idiotype to be regulated by a distinct idiotype network from those ofother mAbs.This publication has 7 references indexed in Scilit:
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