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Kinetic characterization of the changes in protein tyrosine phosphorylation of membranes, cytosolic Ca2+ concentration and viability in boar sperm populations selected by binding to oviductal…

• Anna M. Petrunkina, Johannes Friedrich, Wolfgang Drommer, Gerd Bicker, Dagmar Waberski, Edda Töpfer-Petersen
• Reproduction
• 2001

On reaching the oviduct, spermatozoa are retained in the isthmic region of the oviduct until ovulation occurs. The essential steps of capacitation are co-ordinated in this region. In this study, a… (More)

Spermadhesins: a new protein family. Facts, hypotheses and perspectives.

• Edda Töpfer-Petersen, A. Romero, +4 authors Julio Calvete
• Andrologia
• 1998

Spermadhesins are a novel family of secretory proteins expressed in the male genital tract of pig, horse and bull. They are major products of the seminal plasma and have been found to be peripherally… (More)

Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities.

• Julio Calvete, Katherine M Mann, +5 authors Edda Töpfer-Petersen
• The Biochemical journal
• 1995

We report the complete amino acid sequence of HSP-1, a major protein isolated from stallion seminal plasma or acid extracts of ejaculated spermatozoa. The protein consists of 121 amino acids… (More)

Isolation and biochemical characterization of a zona pellucida-binding glycoprotein of boar spermatozoa.

• Věra Jonáková, Lorena Sanz, Julio Calvete, Agnes H. Henschen, Dana Čechová, Edda Töpfer-Petersen
• FEBS letters
• 1991

Lectin-like molecules on the sperm surface are implicated in the process of gamete recognition and adhesion. We have isolated and biochemically characterized a 15 kDa glycoprotein from ejaculated… (More)

The role of stallion seminal proteins in fertilisation.

• Edda Töpfer-Petersen, Mahnaz Ekhlasi-Hundrieser, Christiane Kirchhoff, Tosso Leeb, Harald Sieme
• Animal reproduction science
• 2005

Seminal plasma proteins are secretory proteins originating mainly from the epididymis and the accessory sex glands. They are involved in the remodelling of the sperm surface which occurs during sperm… (More)

Equine CRISP-3: primary structure and expression in the male genital tract.

• Alexandra Schambony, Marc Gentzel, Heiner Wolfes, Manfred Raida, Uwe Neumann, Edda Töpfer-Petersen
• Biochimica et biophysica acta
• 1998

Although originally described in the male rodent genital tract, cysteine-rich secretory proteins (CRISPs) are expressed in a variety of mammalian tissue and cell types. The proteins of the male… (More)

Boar spermadhesin PSP-II: location of posttranslational modifications, heterodimer formation with PSP-I glycoforms and effect of dimerization on the ligand-binding capabilities of the subunits.

• Julio Calvete, Katherine M Mann, Wolfgang M. Schaefer, Manfred Raida, Lorena Sanz, Edda Töpfer-Petersen
• FEBS letters
• 1995

Spermadhesin PSP-II was isolated from the non-heparin-binding fraction of boar seminal plasma; its disulphide bridge pattern, and the location of a single N-glycosylation site were established.… (More)

Glycosylated boar spermadhesin AWN-1 isoforms. Biological origin, structural characterization by lectin mapping, localization of O-glycosylation sites, and effect of glycosylation on ligand binding.

• Julio Calvete, Dave S Solis, Lorena Sanz, Teresa Diaz-Maurino, Edda Töpfer-Petersen
• Biological chemistry Hoppe-Seyler
• 1994

Spermadhesin AWN-1 is a 133-residues boar sperm surface lectin with capability to bind different ligands, e.g. glycoproteins from zona pellucida (ZP), soybean trypsin inhibitor and heparin, and is… (More)

Effect of glycosylation on the heparin-binding capability of boar and stallion seminal plasma proteins.

• Julio Calvete, M. Reinert, Lorena Sanz, Edda Töpfer-Petersen
• Journal of chromatography. A
• 1995

Boar and stallion seminal plasmas were fractionated using affinity chromatography on heparin-Sepharose. In both species, among other proteins, the heparin-binding (H+) and non-heparin-binding (H-)… (More)

Isolation and characterization of heparin- and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1.

• Julio Calvete, Manfred Raida, Marc Gentzel, Claus Urbanke, Lorena Sanz, Edda Töpfer-Petersen
• FEBS letters
• 1997

In the bovine, seminal plasma heparin-binding proteins bind to sperm lipids containing the phosphorylcholine group and mediate the capacitating effects of heparin-like glycosaminoglycans during sperm… (More)

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