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Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/18554

Title: Isolation and partial characterization of Ca2+-independent lectin from Aedes caspius (Diptera: Culicidae)
Authors: Hassan Ayaad, Tahany.
Keywords: Lectin – Gel gel filtration chromatography - Aedes caspius mosquito – Amino acid analysis
Issue Date: 2008
Publisher: Efflatounia, 8 :17 – 28.
Abstract: Abstract A lectin, designated as ACL, was identified in the body homogenate of the mosquito Aedes caspius by agglutination and sugar inhibition tests. With the use of (NH4)2SO4 fractionation, anion-exchange, and gel filtration chromatography, ACL was purified to homogeneity. The estimated molecular weight of ACL was 68 kDa by gel filtration. The ACL was separated by SDS/PAGE, under non-reducing conditions, as one band of 34 KDa subunits, and as two bands of 32 and 34 kDa under reducing conditions. Isoelectric focusing revealed ACL as a single band at pH 6.5. Amino acid analysis revealed that ACL is an acidic protein in nature. The isolated ACL is a glycoprotein, with the sugar moiety representing 5.5% and contains galactose and mannose as the monosacchride types. ACL is inhibited to a high extent (IC50= 12 mM) by N-acetyl-D-galactosamine, and to a lower extent (IC50= 50-100 mM) by other few sugars. Erythrocyte specificities showed that ACL is specific for sheep, followed by human type-B– RBCs. The hemagglutinating activity (HA) of both crude and isolated lectin are Ca2+-independent. The ACL was heat resistant below 75 °C.
URI: http://hdl.handle.net/123456789/18554
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