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[Purification and study of carbohydrate specificity of lectin from Sarcoscypha coccinea (Fr.) Lambette].
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[Purification and study of carbohydrate specificity of lectin from Sarcoscypha coccinea (Fr.) Lambette].

Author: VO Antoniuk
Edition/Format: Article Article : Ukrainian
Publication:Ukrains'kyi biokhimichnyi zhurnal (1999 ) 2005 May-Jun; 77(3): 96-103
Summary:
A lectin that revealed affinity for lactose, N-acethylactosamine, 4-nitrophenyl-beta-D-gluco- and galactopyranosides from fruiting bodies of Sarcoscypha coccinea (Fr.) Lambette was purified by affinity chromatography on immobilized ovomucoid. According to electrophoresis data in 15% SDS-PAGE the lectin contains two very low-differing components with molecular weight 32 kDa. Molecular weight of the lectin is 128 kDa  Read more...
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Document Type: Article
All Authors / Contributors: VO Antoniuk
Language Note: Ukrainian
Unique Identifier: 107461066
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Abstract:

A lectin that revealed affinity for lactose, N-acethylactosamine, 4-nitrophenyl-beta-D-gluco- and galactopyranosides from fruiting bodies of Sarcoscypha coccinea (Fr.) Lambette was purified by affinity chromatography on immobilized ovomucoid. According to electrophoresis data in 15% SDS-PAGE the lectin contains two very low-differing components with molecular weight 32 kDa. Molecular weight of the lectin is 128 kDa according to gel-chromatography on sephadex G-200. The lectin agglutinates rabbit erythrocytes and slightly weaker agglutinates human erythrocytes. After dialysis against 1% EDTA sodium salt solution the lectin loses hemaglutinating activity, but after the next dialysis against CaCl2 solution it is restored.

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