DC Field | Value | Language |
dc.contributor.author | Meyer, C | |
dc.contributor.author | Schmid, R | |
dc.contributor.author | Schmieding, K | |
dc.contributor.author | Falkenstein, E | |
dc.contributor.author | Wehling, M | |
dc.date.accessioned | 2021-12-23T16:14:24Z | - |
dc.date.available | 2021-12-23T16:14:24Z | - |
dc.date.issued | 1998 | |
dc.identifier.issn | 0039128X | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/11055 | - |
dc.description.abstract | 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. | |
dc.language.iso | en | |
dc.publisher | ELSEVIER SCIENCE INC | |
dc.relation.ispartof | STEROIDS | |
dc.subject | ACROSOME REACTION | |
dc.subject | binding site(s) | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | BRAIN | |
dc.subject | CELLS | |
dc.subject | Endocrinology & Metabolism | |
dc.subject | HUMAN-SPERM | |
dc.subject | liver membrane | |
dc.subject | peptide-specific antiserum | |
dc.subject | PHASE-SEPARATION | |
dc.subject | PLASMA-MEMBRANE | |
dc.subject | progesterone | |
dc.subject | PURIFICATION | |
dc.subject | RAT-LIVER | |
dc.subject | SITES | |
dc.subject | TRITON X-114 | |
dc.title | Characterization of high affinity progesterone-binding membrane proteins by an anti-peptide antiserum | |
dc.type | journal article | |
dc.identifier.doi | 10.1016/S0039-128X(97)00143-8 | |
dc.identifier.isi | ISI:000072074300009 | |
dc.description.volume | 63 | |
dc.description.issue | 2 | |
dc.description.startpage | 111 | |
dc.description.endpage | 116 | |
dc.publisher.place | 655 AVENUE OF THE AMERICAS, NEW YORK, NY 10010 USA | |
dcterms.isPartOf.abbreviation | Steroids | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.orcid | 0000-0003-0851-2767 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | MeCa197 | - |