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Heteromeric nature of glucocorticoid receptor
Author(s) -
Gehring Ulrich,
Arndt Holger
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80208-8
Subject(s) - receptor , glucocorticoid receptor , steroid , photoaffinity labeling , chemistry , glucocorticoid , chymotrypsin , biochemistry , steroid hormone , trypsin , biology , endocrinology , hormone , enzyme
The wild‐type and a mutant receptor of S49.1 lymphoma cells have been shown by photoaffinity labelling to contain steroid‐binding polypeptides of M r 94 000 and 40 000, respectively. We investigated the molybdate‐stabilized forms of these receptors and obtained M r 325 000 and 285 000, respectively, by gel filtration and sedimentation analysis. Mild chymotrypsin treatment of the large wild‐type receptor resulted in a form of about M r 290 000 which contained a steroid‐binding polypeptide of M r 40 000. The data suggest that the high‐ M r forms of glucocorticoid receptors are heteromeric in nature and contain one steroid‐binding polypeptide per complex