Please use this identifier to cite or link to this item: https://doi.org/10.1046/j.1432-1327.1999.00513.x
Title: Detection and characterization of a mannan-binding lectin from the mosquito, Anopheles stephensi (Liston)
Authors: Chen, C. 
Billingsley, P.F.
Keywords: Affinity chromatography
An. stephensi
Lectin
Mosquito
Protein purification
Issue Date: 15-Jul-1999
Citation: Chen, C., Billingsley, P.F. (1999-07-15). Detection and characterization of a mannan-binding lectin from the mosquito, Anopheles stephensi (Liston). European Journal of Biochemistry 263 (2) : 360-366. ScholarBank@NUS Repository. https://doi.org/10.1046/j.1432-1327.1999.00513.x
Abstract: Two lectins from the serum of the mosquito, Anopheles stephensi (Liston), with distinct characteristics, were detected by agglutination of various animal erythrocytes. The lectins were developmental stage-specific and/or sex-related. One adult female-specific lectin was identified as mannan-specific, and named mosquito mannan-binding lectin (MBL). MBL cross- reacted immunologically with antibodies against a previously characterized cockroach lectin, Blaberus discoidalis lectin (BDL1), and its activity was almost completely blocked by the antibodies. Mosquito MBL agglutinated erythrocytes from human, sheep, goat and rabbit, but not chicken or mouse, and agglutination was inhibited by mannan and nitrophenol-modified sugar derivatives, but not by simple sugars. Using affinity chromatography with immobilized mannan on Sepharose 6B, the mosquito MBL was partially purified. Purified mosquito MBL shared biochemical properties with BDL1, containing two subunits of molecular mass of 28 and 30 kDa under reducing conditions in SDS/PAGE. Its activity is dependent on Ca2+, and it is stable at pH 7-9 and at temperatures less than 30 °C.
Source Title: European Journal of Biochemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/100426
ISSN: 00142956
DOI: 10.1046/j.1432-1327.1999.00513.x
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