ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)
"Biotechnologia Acta" v. 6, no. 3, 2013
https://doi.org/10.15407/biotech6.03.069
Р. 69-74, Bibliography 19, Ukrainian.
Universal Decimal classification: 547.963.1:543.9
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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