Inhibition of acrosine-like protease activity by a lectin affinity chromatographic bovine seminal plasma fraction containing the PDC-109 and aSFP proteins
| Autor: | J. M. Scacciati de Cerezo, A. M. Andreetta, M.G. Menesini Chen, J. S. Chen, C. Wolfenstein Todel, A. C. Marquínez |
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| Rok vydání: | 2000 |
| Předmět: |
Male
Glycan Seminal Plasma Proteins medicine.medical_treatment Chromatography Affinity chemistry.chemical_compound Affinity chromatography Semen Lectins Endopeptidases medicine Animals Protease Inhibitors Asparagine Amino Acid Sequence Protease Chromatography biology Chemistry Lectin Proteins Biological activity General Chemistry Molecular biology Biochemistry biology.protein Chromatography Gel Agarose Cattle Electrophoresis Polyacrylamide Gel |
| Zdroj: | Journal of chromatography. B, Biomedical sciences and applications. 746(2) |
| ISSN: | 1387-2273 |
| Popis: | These studies showed that the fractionation of bovine seminal plasma based on lectin agarose affinity chromatography, employing lectins specific to asparagine linked oligosaccharides, and a lectin specific for fucosylated glycans, lead to products with an inhibitory effect on the acrosine-like protease activity. This effect decreases when glycocompounds containing fucosylated Lewis(x) structures are removed, suggesting that these compounds might have some role in the modulation of this activity in the bull. In the fraction devoid of high mannose, hybrid and non-bisecting lactosaminic oligosaccharide-containing glycocompounds, PDC-109 and aSFP proteins were detected and characterized at microscale. |
| Databáze: | OpenAIRE |
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