Particulate fractions of guinea-pig thyroid homogenate contained a single class of receptors which bound 125I-labelled bovine thyrotrophin (TSH) by a saturable, reversible process with an affinity constant of 2 × 109 1/mol. The binding process was specific for TSH, and corresponded with the activation of adenylate cyclase. Cleavage of hormone—receptor bonds by treatment with lyotropic agents resulted in the release of unchanged labelled TSH. The radioligand receptor assay system was sensitive to 0·015 mu. TSH. Bovine or mouse thyroid showed reduced binding affinity with correspondingly reduced sensitivity.
Journal of Endocrinology is committed to supporting researchers in demonstrating the impact of their articles published in the journal.
The two types of article metrics we measure are (i) more traditional full-text views and pdf downloads, and (ii) Altmetric data, which shows the wider impact of articles in a range of non-traditional sources, such as social media.
More information is on the Reasons to publish page.
| Sept 2018 onwards | Past Year | Past 30 Days | |
|---|---|---|---|
| Full Text Views | 6 | 6 | 0 |
| PDF Downloads | 1 | 0 | 0 |
Online ISSN: 1479-6805
Print ISSN: 0022-0795
Strengthening biomedical communities
to advance science and health
CONTACT US
Bioscientifica Ltd | Starling House | 1600 Bristol Parkway North | Bristol BS34 8YU | UK
Bioscientifica Ltd | Registered in England no 3190519
