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- W1436904535 abstract "[3H]Triamcinolone acetonide was used to tag covalently specific glucocorticoid receptors by photoaffinity labelling at lambda greater than or equal to 320 nm. Receptors of wild-type mouse lymphoma cells and two glucocorticoid resistant mutants of nuclear transfer deficient (nt-) and increased nuclear transfer (nti) phenotypes, respectively, were used. Wild-type and nt- receptors yielded radiolabelled polypeptide bands of mol. wt. 98 000 as revealed by gel electrophoresis under denaturing conditions and fluorography. In contrast, the nti receptor had a mol. wt. of 42 000. Partial proteolysis of the wild-type receptor with alpha-chymotrypsin resulted in a fragment of mol. wt. 39 000 which still contained the steroid binding site but had increased affinity for DNA indistinguishable from that of the nti receptor. Chymotrypsin thus removed a domain from the wild-type receptor polypeptide which is involved in modulating DNA binding. The same domain is missing from the nti receptor." @default.
- W1436904535 created "2016-06-24" @default.
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- W1436904535 date "1982-03-01" @default.
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- W1436904535 title "Active domains in wild-type and mutant glucocorticoid receptors." @default.
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- W1436904535 doi "https://doi.org/10.1002/j.1460-2075.1982.tb01161.x" @default.
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