Abstract
A new lectin with 6.5 mg/kg yield was purified from fresh bulb Hyacinthella аcutiloba K. Perss. by combination of affinity chromathography on yeast mannan and by ion exchange chromatography on DEAE-toyopearl. The best lectin inhibitor among tested monoand disaccharides was D-turanose (Glcp α1-3 Fruf). Very powerful inhibitor of lectin activity was yeast mannan. The lectin revealed weak affinity to α-methyl-Dmannoside, D-fructose and 2-acetamido-D-galactopyranoside. The lectin interacted also with pig liver glycogen, starch and mannose-containing glycoproteins (ovoalbumin, ovomucoid and calf thyroglobulin), but don’t interacted with horsera dish peroxidase and calf intestine alkaline phosphatase. According to electrophoresis, in 20% SDS-PAAG containing SDS-Na the lectin consists with subunits of molecular weight 12 kDa. Molecular weight of the lectin is 48 kDa according to gel-chromatography on Toyopearl HW-55. The lectin agglutinated best of all rabbit erythrocytes and worse agglutinated guinea-pig, very weak — rat erythrocytes and did not agglutinate human and goat erythrocytes. After dialysis against 1% EDTA sodium salt solution the lectin did not lose hemaglutinating activity and endured heating to +65 °C during one hour.
Highlights
A new lectin with 6.5 mg/kg yield was purified from fresh bulb Hyacinthella аcutiloba K
In 20% SDS-PAAG containing SDS-Na the lectin consists with subunits of molecular weight 12 kDa
Molecular weight of the lectin is 48 kDa according to gelchromatography on Toyopearl HW-55
Summary
A new lectin with 6.5 mg/kg yield was purified from fresh bulb Hyacinthella аcutiloba K. Universal Decimal classification: 547.963.1:543.9 PURIFICATION AND CHARACTERIZATION OF A NEW MANNOSE-SPECIFIC LECTIN FROM Hyacinthella аcutiloba K.
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