Literature DB >> 6282674

Evidence that the porcine thyrotropin (TSH) receptor contains an essential disulphide bridge.

J Ginsberg, B R Smith, R Hall.   

Abstract

The effects of reducing agents on membrane bound and detergent solubilised porcine TSH receptors have been investigated. Both 2-mercaptoethanol and dithiothreitol appeared to inhibit the TSH-binding activity by a direct effect on the TSH receptor itself and Scatchard analysis suggested that this was primarily due to an alteration in TSH-binding capacity. In addition, some binding activity could be recovered by reoxidation of reduced receptor preparations. These results suggest therefore that the porcine TSH receptor contains an essential disulphide bridge.

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Year:  1982        PMID: 6282674     DOI: 10.1016/0303-7207(82)90008-9

Source DB:  PubMed          Journal:  Mol Cell Endocrinol        ISSN: 0303-7207            Impact factor:   4.102


  2 in total

1.  Interaction of autoantibodies to thyrotropin receptor with a hydrophilic subunit of the thyrotropin receptor.

Authors:  E Davies Jones; F A Hashim; Y Kajita; F M Creagh; P R Buckland; V B Petersen; R D Howells; B Rees Smith
Journal:  Biochem J       Date:  1985-05-15       Impact factor: 3.857

2.  Structure of the porcine thyrotropin receptor: a 200 kilodalton glycoprotein heterocomplex.

Authors:  M N Islam; N R Farid
Journal:  Experientia       Date:  1985-01-15
  2 in total

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