Inhibition of acrosine-like protease activity by a lectin affinity chromatographic bovine seminal plasma fraction containing the PDC-109 and aSFP proteins.

Autor: Marquínez AC; Centro de Investigaciones en Reproducción, Facultad de Medicina, Paraguay, Buenos Aires, Argentina., Andreetta AM, Chen JS, Menesini Chen MG, Wolfenstein Todel C, Scacciati de Cerezo JM
Jazyk: angličtina
Zdroj: Journal of chromatography. B, Biomedical sciences and applications [J Chromatogr B Biomed Sci Appl] 2000 Sep 15; Vol. 746 (2), pp. 141-50.
DOI: 10.1016/s0378-4347(00)00308-x
Abstrakt: 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: MEDLINE
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