title: Purification of an ovine, androgen-dependent epididymal protein. Evidence for a strong amino acid sequence homology with serum albumin.
abstract: An ovine, testosterone-dependent protein was purified from an extract of epididymides of orchidectomized-, testosterone-implanted rams by ethylene glycol precipitation, anion exchange chromatography, preparative non-denaturing PAGE at alkaline pH and gel filtration. The protein which had previously been named ovine prealbumin-epididymis-specific protein (oPES), migrated as a single band ahead of ovine serum albumin (oSA). A single component, with an apparent MW of 60 kDa, lower than that of oSA, was also observed in SDS-PAGE. oPES was cleaved after lysyl residues using endoproteinase Lys-C and the hydrolysate was fractionated in 2 steps by reverse-phase HPLC. Six oligopeptides were recovered and sequenced. They all displayed complete identity with regions of bovine serum albumin scattered in the two-third N-terminal part. However, in 2 of them, there was no complete identity with homologous parts of oSA. This indicates that oPES and oSA are probably encoded by different genes.
authors.affiliation: INRA Bât 224, Unité Protéines, Jouy-en-Josas, France.
authors.forename: C
authors.initials: C
authors.lastname: Carles
authors.forename: S
authors.initials: S
authors.lastname: Fournier-Delpech
authors.forename: B
authors.initials: B
authors.lastname: Ribadeau-Dumas
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002845:Chromatography; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004822:Epididymis / Q000737:chemistry*; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D009919:Orchiectomy; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*; D051381:Rats; D017386:Sequence Homology, Amino Acid; D012709:Serum Albumin / Q000737:chemistry*; D012756:Sheep; D013739:Testosterone / Q000494:pharmacology*
chemical_list: D011506:Proteins; D012709:Serum Albumin; D013739:Testosterone