In:
FEBS Letters, Wiley, Vol. 150, No. 2 ( 1982-12-27), p. 347-353
Abstract:
Using a modified charcoal method, we could detect a steroid‐binding component in rat lung cytosol which specifically binds R5020, progesterone, and some of its natural derivatives. The concentration of binding sites is high (30–40 pmol/mg protein), the affinity is moderate, the K d of the R5020 complex being ∼10 −7 M. Proteolytic enzymes and sulfhydryl reagents destroyed the binding sites indicating the protein nature and the requirement for disulfide bonds. The protein sedimented in the 2 S range thus had an M r of 10 000–15 000. Further characteristics are the extreme heat (30 min at 100°C) and acid (pH 1) stability. These properties and the fact that it was not detected in serum, distinguish this binding protein from receptors and specific serum steroid binders.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(82)80766-7
Language:
English
Publisher:
Wiley
Publication Date:
1982
detail.hit.zdb_id:
1460391-3
SSG:
12
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