Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities
| Autor: | Karlheinz Mann, Manfred Raida, Edda Töpfer-Petersen, S. Nessau, Markus Reinert, Juan J. Calvete, Wolfram Schäfer, Libia Sanz |
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| Přispěvatelé: | Ministerium für Innovation, Wissenschaft und Forschung des Landes Nordrhein-Westfalen, Dirección General de Investigación Científica y Técnica, DGICT (España) |
| Rok vydání: | 1995 |
| Předmět: |
Male
Glycosylation Seminal Plasma Proteins Molecular Sequence Data Oligosaccharides Biology Biochemistry Chromatography Affinity chemistry.chemical_compound Semen Lectins Carbohydrate Conformation Animals Amino Acid Sequence Horses Binding site Molecular Biology Peptide sequence Chromatography High Pressure Liquid Glycoproteins chemistry.chemical_classification Binding Sites Sequence Homology Amino Acid Heparin Prostatic Secretory Proteins Proteins Cell Biology Oligosaccharide Molecular biology Amino acid chemistry Carbohydrate Sequence Gelatin Carbohydrate conformation Glycoprotein Carrier Proteins Research Article |
| Zdroj: | Europe PubMed Central Scopus-Elsevier CIÊNCIAVITAE Digital.CSIC. Repositorio Institucional del CSIC instname |
| ISSN: | 0264-6021 |
| Popis: | 8 pags, 6 figs, 2 tabs 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 organized in two types of homologous repeats arranged in the pattern AA'BB'. Each of the 13-15-residue A-type repeats contains two O-linked oligosaccharide chains. The B-type repeats span 44-47 amino acids each, are not glycosylated, and have the consensus pattern of the gelatin-binding fibronectin type-II module. This domain also occurs in the major bovine seminal plasma heparin-binding proteins PDC-109 (BSP-A1/A2) and BSP-A3. However, unlike the bovine proteins which bind quantitatively to a heparin-Sepharose column, stallion HSP-1 was recovered in both the flow-through and the heparin-bound fractions. Structural analysis showed that the two HSP-1 forms contain identical polypeptide chains which are differently glycosylated. Moreover, size-exclusion chromatography showed that heparin-bound HSP-1 associates with HSP-2, another major seminal plasma protein, into a 90 kDa product, whereas the non-heparin-bound glycoform of HSP-1 is eluted as a monomeric (14 kDa) protein. This suggests that glycosylation may have an indirect effect on the heparin-binding ability of HSP-1 through modulation of its aggregation state. On the other hand, both glycoforms of HSP-1 displayed gelatin-binding activity, indicating that the molecular determinants for binding heparin and gelatin are different. This work was financed by grants 01 KY9103 from Bundesministerium fur Forschung und Technologie, Bonn, Germany (to E.T.-P.) and PB92-0096 from Dirección General de Investigación Científica y Técnica, Madrid, Spain (to J.J.C. and L.S.). |
| Databáze: | OpenAIRE |
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