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Your search keyword '"Töpfer-Petersen, Edda"' showing total 24 results
Start Over Author "Töpfer-Petersen, Edda" Publisher elsevier bv
24 results on '"Töpfer-Petersen, Edda"'

6. Evolution of the spermadhesin gene family

Author

Haase, Bianca, primary, Schlötterer, Christian, additional, Hundrieser, Mahnaz Ekhlasi, additional, Kuiper, Heidi, additional, Distl, Ottmar, additional, Töpfer-Petersen, Edda, additional, and Leeb, Tosso, additional

Published
2005
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9. Molecular characterization of the equine testis-specific protein 1 ( TPX1 ) and acidic epididymal glycoprotein 2 ( AEG2 ) genes encoding members of the cysteine-rich secretory protein (CRISP) family

Author

Giese, Alexander, primary, Jude, Rony, additional, Kuiper, Heidi, additional, Raudsepp, Terje, additional, Piumi, Francois, additional, Schambony, Alexandra, additional, Guérin, Gérard, additional, Chowdhary, Bhanu P., additional, Distl, Ottmar, additional, Töpfer-Petersen, Edda, additional, and Leeb, Tosso, additional

Published
2002
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10. Molecular characterization of the equine AEG1 locus

Author

Giese, Alexander, primary, Jude, Rony, additional, Kuiper, Heidi, additional, Piumi, Francois, additional, Schambony, Alexandra, additional, Guérin, Gérard, additional, Distl, Ottmar, additional, Töpfer-Petersen, Edda, additional, and Leeb, Tosso, additional

Published
2002
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11. Crystallization and preliminary X-ray diffraction analysis of boar seminal plasma spermadhesin PSP-I/PSP-II, a heterodimer of two CUB domains

Author

Dirección General de Investigación Científica y Técnica, DGICT (España), Romero, Antonio, Fernández-Varela, Paloma, Sanz, Libia, Töpfer-Petersen, Edda, Calvete, Juan J., Dirección General de Investigación Científica y Técnica, DGICT (España), Romero, Antonio, Fernández-Varela, Paloma, Sanz, Libia, Töpfer-Petersen, Edda, and Calvete, Juan J.

Abstract

Boar spermadhesin PSP-I/PSP-II (M(r) 29,000-30,000), a non-covalent heterodimer of two CUB domains, was crystallized in two crystal forms. Complete diffraction data sets for hexagonal (space group P61,522) and trigonal (space group P31,221) crystals have been collected up to 2.9 and 2.5 Å resolution, respectively. Cell constants of the hexagonal and trigonal crystal forms are a = b = 87.2 Å, c = 152.4 Å, and a = b = 96.2 Å, c = 70.8 Å, respectively. The calculated packing parameters (V(m)) are 2.8 and 3.2 Å3/Da for the hexagonal and trigonal crystal forms, respectively, indicating that, in both cases, the asymmetric unit is constituted by one PSP-I/PSP-II heterodimer. This paper reports the first crystals of a protein built up by a CUB domain architecture.

Published
1996

12. 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

Author

Dirección General de Investigación Científica y Técnica, DGICT (España), Calvete, Juan J., Mann, K., Schäfer, Wolfram, Raida, Manfred, Sanz, Libia, Töpfer-Petersen, Edda, Dirección General de Investigación Científica y Técnica, DGICT (España), Calvete, Juan J., Mann, K., Schäfer, Wolfram, Raida, Manfred, Sanz, Libia, and Töpfer-Petersen, Edda

Abstract

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. PSP-II forms a heterodimer with specific N-glycoforms of PSP-I. Although both subunits possess heparin-binding capability, the PSP-I/PSP-II complex does not. The heterodimer contains binding sites for zona pellucida glycoproteins and soybean trypsin inhibitor located in the PSP-II subunit. However, the PSP-I/PSP-II heterodimer binds only loosely to the sperm surface and is easily removed during in vitro capacitation, suggesting that the zona pellucida binding activity may not be relevant for gamete interaction. Our results show that dimerization of spermadhesins PSP-I and PSP-II markedly affects their binding capabilities. © 1995.

Published
1995

14. Characterization of AWN-1 glycosylated isoforms helps define the zona pellucida and serine proteinase inhibitor-binding region on boar spermadhesins

Author

Dirección General de Investigación Científica y Técnica, DGICT (España), Calvete, Juan J., Sanz, Libia, Dostàlovà, Z., Töpfer-Petersen, Edda, Dirección General de Investigación Científica y Técnica, DGICT (España), Calvete, Juan J., Sanz, Libia, Dostàlovà, Z., and Töpfer-Petersen, Edda

Abstract

Spermadhesin AWN-1 (14 kDa) belongs to a recently described family of boar sperm surface-associated proteins. AWN-1 is a multifunctional protein which possesses heparin-, serine proteinase inhibitor-, and zona pellucida glycoprotein-binding capability. Therefore it has been implicated in sperm capacitation and sperm-oocyte attachment. Here, we report the characterization of 22-25 kDa isoforms of AWN-1 isolated by heparin-affinity chromatography, which fail to bind to zona pellucida glycoproteins or serine proteinase inhibitors. Our results show that the structure of the high and low molecular mass AWN-1 forms differ in that the former is N-glycosylated at Asp50 and truncated at the C-terminus. The inability of the glycosylated AWN-1 molecules to bind ligands is due solely to the presence of the oligosaccharide moieties, however. This indicates that glycosylation of AWN-1 may modulate its ligand-binding capabilities. On the other hand, the effect of glycosylation on ligand-binding suggests that both the zona pellucida- and the serine proteinase inhibitor binding domain(s) may be located around the glycosylation point. © 1993.

Published
1993

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