Characterization of high affinity progesterone-binding membrane proteins by an anti-peptide antiserum
Autor(en): | Meyer, C Schmid, R Schmieding, K Falkenstein, E Wehling, M |
Stichwörter: | ACROSOME REACTION; binding site(s); Biochemistry & Molecular Biology; BRAIN; CELLS; Endocrinology & Metabolism; HUMAN-SPERM; liver membrane; peptide-specific antiserum; PHASE-SEPARATION; PLASMA-MEMBRANE; progesterone; PURIFICATION; RAT-LIVER; SITES; TRITON X-114 | Erscheinungsdatum: | 1998 | Herausgeber: | ELSEVIER SCIENCE INC | Journal: | STEROIDS | Volumen: | 63 | Ausgabe: | 2 | Startseite: | 111 | Seitenende: | 116 | Zusammenfassung: | A chemically synthesized 15-mer oligopeptide derived from the N terminus of high affinity progesterone-binding membrane site(s) from porcine liver was used to generate site-specific antibodies. Western blotting experiments confirmed the specificity of the anti-peptide serum obtained. In further investigations this antiserum was used for identification of the native progesterone-binding membrane protein complex that represents an oligomer with an apparent molecular mass of about 200 kDa. In temperature-induced Triton X-114 phase separation experiments combined with Western-blotting, the progesterone-binding site was identified as an hydrophobic (integral) membrane protein. In addition, in Western blotting analyses the antiserum reacted with the progesterone-binding or related proteins in membrane fractions from a wide array of different tissues in various species. (C) 1998 by Elsevier Science Inc. |
ISSN: | 0039128X | DOI: | 10.1016/S0039-128X(97)00143-8 |
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