Purification and primary structure of a new bovine spermadhesin.
Z13 is a new seminal plasma protein made up of two disulfide-linked 13-kDa subunits that was identified in our laboratory by 2D PAGE. In this report we present the purification of Z13 from bovine seminal plasma. In solution, the protein is a nonglycosylated dimer that presents one interchain disulfide bond and does not show heparin-binding properties. The complete primary structure and the localization of the S-S bridges are reported. The results suggest that Z13 is a new protein of the spermadhesin family whose members are thought to play a prominent role in different aspects of fertilization.
Tedeschi
G
G
Istituto di Fisiologia Veterinaria e Biochimica, Milano, Italy. gabriella.tedeschi@unimi.it
Oungre
E
E
Mortarino
M
M
Negri
A
A
Maffeo
G
G
Ronchi
S
S
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D017124:Conserved Sequence; D004220:Disulfides / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D008297:Male; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012661:Semen / Q000737:chemistry*; D029589:Seminal Plasma Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D004220:Disulfides; D010446:Peptide Fragments; D011506:Proteins; D029589:Seminal Plasma Proteins; C425042:spermadhesin