ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)
"Biotechnologia Acta" v. 6, no. 3, 2013
Р. 69-74, Bibliography 19, Ukrainian.
Universal Decimal classification: 547.963.1:543.9
PURIFICATION AND CHARACTERIZATION
OF A NEW MANNOSE-SPECIFIC LECTIN FROM Hyacinthella аcutiloba K. Perss.
V. O. Antonyuk1, 2, L. V. Panchak1,2, M. O. Starykovych1,
K. S. Strutovskaya2, R. S. Stoika1
1Institute of Cell Biology of National Academy of Sciences of Ukraine, Lviv
2Danylo Halytsky Lviv National Medical University, Ukraine
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 mono- and disaccharides was D-turanose (Glcp ?1-3 Fruf). Very powerful inhibitor of lectin activity was yeast mannan. The lectin revealed weak affinity to ?-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 gelchromatography 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.
Key words: mannose-specific lectins, Hyacinthella аcutiloba, purification, properties.
© Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine, 2013
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