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- Title
Isolation and characterization of lectin from the surface of Grifola frondosa (Fr.) S.F.Gray mycelium.
- Authors
Stepanova, L. V.; Nikitina, V. E.; Boiko, A. S.
- 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-Rha p-(1→3)-α- D-Rha p-(1→3)-α- D-Rha p-(1→2)-α- D-Rha p-(1→2)-α-s D-Rha p-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.
- Subjects
LECTINS; MAITAKE; MYCELIUM; BASIDIOMYCETES; GLYCOPROTEINS; ERYTHROCYTES; BLOOD groups; TRYPSIN; BLOOD agglutination; AMINO acids
- Publication
Microbiology (00262617), 2007, Vol 76, Issue 4, p429
- ISSN
0026-2617
- Publication type
Article
- DOI
10.1134/S0026261707040078