The major Kurloff cell glycoproteins: lectin affinities, glycosidase susceptibilities and relationship with the sialylated acid phosphatases of the Kurloff body
| Autor: | Slim-Eric Letaïef, Gérard Landemore, N. Oulhaj, Jacques Izard |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Male
PNGase F Kurloff cell Glycoside Hydrolases Glycoconjugate Cells Acid Phosphatase Guinea Pigs Molecular Sequence Data Biophysics Cell Separation Sialidase Biochemistry Chromatography DEAE-Cellulose chemistry.chemical_compound Lectins Animals Molecular Biology Glycoproteins chemistry.chemical_classification biology Lectin biology.organism_classification Molecular biology Sialic acid Molecular Weight Carbohydrate Sequence chemistry Canavalia ensiformis Sialic Acids biology.protein Electrophoresis Polyacrylamide Gel Female Glycoprotein Spleen |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 1116:112-121 |
| ISSN: | 0304-4165 |
| Popis: | Urea-soluble fractions from purified Kurloff cells (KC) were analysed by affinoblotting. Lectin reactivities were quasi-exclusively confined to the 30-35 kDa major glycoproteins (mGPs) (responsible for the PAS positivity of the Kurloff body) with strong affinities for Canavalia ensiformis lectin, Phaseolus vulgaris erythroagglutinin and Sambucus nigra (SNA), Pisum sativum, Triticum vulgaris and Ulex europeus agglutinins. These data were consistent with the presence, among the KC mGPs, of large amounts of complex or hybrid N-glycosylproteins, in particular with Neu5Ac alpha 2,6Gal/GalNAc sequences, fucosyl residues and bisected residues. Their oligosaccharide sequences belong to more than one class, since some of these lectin reactivities had to be borne by distinct N-linked oligosaccharide chains. Before further analysis, KC mGPs were separated from other highly anionic glycoconjugates, by DEAE-cellulose chromatography. Their abundant potential RCA-binding sites masked by sialic acid were then revealed after neuraminidase (sialidase) or dilute acid pre-treatment. In remaining consistent with their lectin affinities, some KC mGPs were found to be PNGase F sensitive, while, either desialylated or not, they were all O-glycanase insensitive. Finally, by combined zymography and affinoblotting, the SNA-reactive fraction of KC mGPs was shown to correspond to denatured forms of the two zymographic size populations (190 kDa and 500 kDa) of KC acid phosphatases. |
| Databáze: | OpenAIRE |
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