Detection of a heat‐ and acid‐stable ‘progesterone’‐binding protein in the rat lung

FEBS Letters

Moser, Ewald H.¹  Daxenbichler, Günter¹ 

[1] Universitätsklinik für Frauenheilkunde Innsbruck, Anichstr. 35, A-6020 Innsbruck, Austria

关键词: Rat;    Lung;    Cytosol;    Protesterone;    Binding protein;   

DOI  :  10.1016/0014-5793(82)80766-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown