Biopolym. Cell. 2009; 25(6):466-475.
Cell Biology
Carbohydrate specificity of lectin, purified from the fruiting bodies of Mycena pura /Fr./ Kumm. and its use in histochemical investigation
1, 2Antonyuk V. O., 2Yastchenko A. M., 2Antonyuk R. V., 2Ambarova N. O.
  1. Institute of Cell Biology, NAS of Ukraine
    14/16, Drahomanov Str., Lviv, Ukraine, 79005
  2. Danylo Halytsky Lviv National Medical University
    69, Pekarska Str., Lviv, Ukraine, 79010


Aim. The purpose of this investigation was to research carbohydrate specificity of a new lectin from fruiting body of Mycena pura and possibilities of its application in histochemical studies. Methods. The lectin has been purified by affinity chromatography on «ovomucine». The lectin carbohydrate specificity has been determined by a reaction of inhibiting haemagglutination by haptens. Histological materials were fixed in 4 % neutral formalin solution. Alkaline phosphatase was revealed in the cryostat unfixed microscopical sections. Results. The lectin yield from fresh fruit bodies of raw material was 9 mg/kg. Mol. mass of the lectin is 40 kDa. The lectin poorly interacted with D-glucose and D-mannose in contrast to lectins from Pisum sativum and Leucojum vernum. The peculiarity of this lectin is its strong interaction with alkaline phosphatase, the highest among twenty tested lectins. However, the receptors for Mycena lectin binding in mammalian tissues are not limited by this enzyme being presented also by glycoconjugates of another structure, as it was shown for fetus calf small intestine and kidney of rat. Conclusions. An important role in the lectin interaction with glycoproteins probably belongs to the disaccharide links of GlcNAcβ(1-2)Manα(1-6) or GlcNAcβ(1- 2)Manα(1-2), which not necessarily are terminal.
Keywords: Mycena pura, lectins, histochemistry, alkaline phosphatase


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