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.

Purification and primary structure of a new bovine spermadhesin / G. Tedeschi, E. Oungre, M. Mortarino, A. Negri, G. Maffeo, S. Ronchi. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - 267:20(2000), pp. 6175-6179. [10.1046/j.1432-1327.2000.01698.x]

Purification and primary structure of a new bovine spermadhesin

G. Tedeschi
Primo
;
E. Oungre
Secondo
;
M. Mortarino;A. Negri;G. Maffeo
Penultimo
;
S. Ronchi
Ultimo
2000

Abstract

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.
Settore BIO/10 - Biochimica
2000
Article (author)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/181371
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