Purification of a candidate gonadotrophin surge attenuating factor from human follicular fluid

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dc.contributor.authorPappa, A.en
dc.contributor.authorSeferiadis, K.en
dc.contributor.authorFotsis, T.en
dc.contributor.authorShevchenko, A.en
dc.contributor.authorMarselos, M.en
dc.contributor.authorTsolas, O.en
dc.contributor.authorMessinis, I. E.en
dc.date.accessioned2015-11-24T18:55:27Z
dc.date.available2015-11-24T18:55:27Z
dc.identifier.issn0268-1161-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18883
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectBiological Assayen
dc.subjectCells, Cultureden
dc.subjectChromatography, High Pressure Liquiden
dc.subjectElectrophoresis, Polyacrylamide Gelen
dc.subjectFemaleen
dc.subjectFollicular Fluid/*chemistryen
dc.subjectGlycosylationen
dc.subjectGonadal Hormonesen
dc.subjectGonadal Steroid Hormones/isolation & purificationen
dc.subjectGonadotropin-Releasing Hormone/pharmacologyen
dc.subjectHot Temperatureen
dc.subjectHumansen
dc.subjectLuteinizing Hormone/secretionen
dc.subjectMolecular Sequence Dataen
dc.subjectPituitary Gland/drug effectsen
dc.subjectProteins/chemistry/*isolation & purification/pharmacologyen
dc.subjectRatsen
dc.subjectSequence Homologyen
dc.titlePurification of a candidate gonadotrophin surge attenuating factor from human follicular fluiden
heal.abstractGonadotrophin surge attenuating factor (GnSAF) is a new non-steroidal ovarian substance, different from inhibin, which attenuates the pre-ovulatory luteinizing hormone (LH) surge in superovulated women. Human follicular fluid (FF) was used as a source for the isolation of GnSAF, the activity of which was monitored in an in-vitro pituitary bioassay. Primary rat pituitary cells were incubated with test substances for 48 h and subsequently washed and incubated with 0.1 micromol/l gonadotrophin releasing hormone (GnRH) plus test substances for 4 h. GnSAF activity was expressed as the reduction of GnRH-induced LH secretion in the 4 h incubation. GnSAF was purified from 250 ml of FF which was heat-treated at 80 degrees C for 5 min. Heparin-sepharose chromatography, Con-A sepharose chromatography, reversed-phase high-performance liquid chromatography (HPLC) and preparative native gel electrophoresis were used for GnSAF fractionation. Using these purification steps, we have obtained an apparently homogeneous preparation that stains as a single band on sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis. GnSAF has an apparent molecular weight of 12.5 kDa and was identified by amino acid sequence (mass spectrometry) to be the C-terminal fragment of human serum albumin.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/10357957-
heal.identifier.secondaryhttp://humrep.oxfordjournals.org/content/14/6/1449.full.pdf-
heal.journalNameHum Reproden
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate1999-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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