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Journal archive > 2007 > N 2 March-April 


L. V. Panchak1, V. О. Antonyuk2

1Danylo Halytsky National Medical University, Lviv;
2Institute of Cell Biology, National Academy of Sciences of Ukraine, Lviv;
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A lectin from fruiting bodies of Lactarius rufus (Scop.: Fr.)Fr. has been purified by affinity chromatography on copolymer of polyvinyl alcohol with a blood group B specific substance. The lectin gives a single band at disk-electrophoresis in acidic­ (рН 4.3) and alkaline (рН 8.6) buffer systems. Under electrophoresis in 10–20% SDS-PAGE, the lectin consists of identical subunits with molecular weight 17 ± 1 kDa. Molecular weight of the lectin is 98 kDa according to gel-chromatography on Tojopearl HW-55. It is supposed that the lectin contains six subunits. The lectin is quite enough stable in рН 4.0–10.0, its activity does not depend upon bivalent metal ions. When heating the lectin solution to 65 °С it lost more than 85% of its activity. The lectin agglutinates human etrythrocytes without any marked group specificity, it agglutinates 2–4 times worse rabbit erythrocytes, very weakly crucian erythrocytes and does not agglutinate sheep erythrocytes. Mono- and disaccharides are not inhibitors of the lectin activity, while ?-phenyl-N-acethyl-D-glucosaminopyranosid (0.08 mM) and 4-nitrophenyl-?-D-glucosamin are the best inhibitors of its activity. Among glycoproteins the best inhibitors of the lectin activity are: group-specific substances from human blood erythrocytes, asialosubmaxillary bovine mucin, human and bovine thyroglobulin and more weak inhibitors are fetuin, transferrin and human Ig G.

Key words: lectins, fungi, Lactarius rufus (Scop.: Fr.)Fr., purification, properties.

The original article in Ukrainian is available for download in PDF format.

© The Ukrainian Biochemical Journal