DC Field | Value | Language |
dc.contributor.author | Meyer, C | |
dc.contributor.author | Schmid, R | |
dc.contributor.author | Scriba, PC | |
dc.contributor.author | Wehling, M | |
dc.date.accessioned | 2021-12-23T16:15:50Z | - |
dc.date.available | 2021-12-23T16:15:50Z | - |
dc.date.issued | 1996 | |
dc.identifier.issn | 00142956 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/11604 | - |
dc.description.abstract | High-affinity progesterone-binding sites have been identified, characterized in and purified from porcine liver membranes. They were functionally solubilized by the non-denaturing zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (Chaps, 20 mM, detergent/protein mass ratio 4:1) at a yield of 75-80%. Using [H-3]progesterone as radioligand, binding studies showed high-affinity and low-affinity binding sites in microsomal preparations with an apparent K-d1, of 11 nM and an apparent K-d2 of 286 mM. In solubilized fractions the high-affinity binding sites were present at an apparent K-d of 69 mM. In both preparations, progesterone binding was time-dependent, saturable, reversible, and showed a similar hierachy of affinities for related steroids. A purification scheme ws developed based on anion-exchanger procedures. The purified fraction as identified by maximum specific progesterone-binding activity contained two major polypeptides of apparent molecular masses (SDS/PAGE) of 28 kDa and 56 kDa, respectively. Sequencing of both polypeptides showed an identical amino terminus without significant identity in the amino acid sequence to any known protein primary structure. | |
dc.language.iso | en | |
dc.publisher | SPRINGER VERLAG | |
dc.relation.ispartof | EUROPEAN JOURNAL OF BIOCHEMISTRY | |
dc.subject | ACROSOME REACTION | |
dc.subject | ALDOSTERONE | |
dc.subject | amino acid sequence | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CELLS | |
dc.subject | HUMAN-SPERM | |
dc.subject | liver | |
dc.subject | membrane-binding site | |
dc.subject | PLASMA-MEMBRANE | |
dc.subject | progesterone | |
dc.subject | PROTEIN | |
dc.subject | RAT-LIVER | |
dc.subject | STEROID-HORMONES | |
dc.subject | VASCULAR SMOOTH-MUSCLE | |
dc.subject | XENOPUS-LAEVIS OOCYTES | |
dc.title | Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes | |
dc.type | journal article | |
dc.identifier.doi | 10.1111/j.1432-1033.1996.0726u.x | |
dc.identifier.isi | ISI:A1996VB01700024 | |
dc.description.volume | 239 | |
dc.description.issue | 3 | |
dc.description.startpage | 726 | |
dc.description.endpage | 731 | |
dc.publisher.place | 175 FIFTH AVE, NEW YORK, NY 10010 | |
dcterms.isPartOf.abbreviation | Eur. J. Biochem. | |
dcterms.oaStatus | Bronze | |
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 | - |