Isolation and characterization of lectin from the surface of Grifola frondosa (Fr.) S.F.Gray mycelium |
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Authors: | L. V. Stepanova V. E. Nikitina A. S. Boiko |
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Affiliation: | (1) Institute of Biochemistry and Physiology of Plants and Microorganisms, Russian Academy of Sciences, Saratov, Russia;(2) Chernyshevskii Saratov State University, Russia |
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Abstract: | From the surface of the dikaryotic mycelium of the xylotrophic basidiomycete Grifola frondosa 0917 a lectin has been isolated with a molecular mass of 68 ± 1 kDa, consisting of two subunits of 33–34 kDa each. The lectin is a hydrophilic glycoprotein with the protein: glycan ratio of 3: 1. It exhibits high affinity to native rabbit erythrocytes and to human erythrocytes of the 0 blood group, but not to trypsin-treated ones. The hemagglutination (HA) caused by lectin was not blocked by any of the 25 tested mono-, di-, and amino sugars; it was also not blocked by some of glyco derivatives. Only 13.9 µg/ml of the homogeneous preparation of a polysaccharide, a linear D-rhamnan with the structure of the repeated component →2)-β-D-Rhap-(1→3)-α-D-Rhap-(1→3)-α-D-Rhap-(1→2)-α-D-Rhap-(1→2)-α-sD-Rhap-1(→ blocked hemagglutination completely. The analysis of the amino acid composition of the lectin showed the greatest percentage of amino acids with positively charged R groups, arginine, lysine, and histidine, as well as the complete absence of sulfurcontaining amino acids, cysteine, and methionine. D-glucose and D-glucosamine were detected in the carbohydrate part. |
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Keywords: | Grifola frondosa mycelial lectin xylotrophic basidiomycete glycoprotein carbohydrate specificity D-rhamnan |
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