Steroid receptors in Streptomyces hydrogenans: isolation and characterization of a high affinity receptor for 5alpha-dihydrotestosterone.
There are different steroid binding receptors in the cytosol of Streptomyces hydrogenans. A high molecular weight component binds 5alpha-dihydrotestosterone (17beta-hydroxy-5alphaH-androstan-3-one) with high affinity. Partial purification is achieved by density gradient centrifugation and filtration on Sephadex G-200. 5alpha-Dihydrotestosterone and progesterone compete for the same binding sites on the receptor. Cyproterone and testosterone are not bound. As it is easy to isolate the binding fraction, a simple assay for 5alpha-dihydrotestosterone or progesterone in biological samples is available.
D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D001665:Binding Sites; D003600:Cytosol / Q000378:metabolism; D013196:Dihydrotestosterone / Q000378:metabolism*; D008970:Molecular Weight; D011374:Progesterone / Q000378:metabolism; D011485:Protein Binding; D013302:Streptomyces / Q000032:analysis / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism
D001426:Bacterial Proteins; D013196:Dihydrotestosterone; D011374:Progesterone