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Effects of physico‐chemical treatments on hemagglutination activity of Anopheles gambiae haemolymph and midgut extract
Author(s) -
MOHAMED HASSAN A.,
INGRAM GEORGE A.
Publication year - 1994
Publication title -
medical and veterinary entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 82
eISSN - 1365-2915
pISSN - 0269-283X
DOI - 10.1111/j.1365-2915.1994.tb00376.x
Subject(s) - hemolymph , biology , agglutinin , midgut , biochemistry , hemagglutination , microbiology and biotechnology , lectin , antibody , botany , immunology , larva
.Anopheles gambiae midgut extracts and haemolymph possessed agglutinins, titre 1:16 to 1:256, against human red blood cells (RBCs). Subjection of both tissues to protein precipitation reagents, organic chemical and selected protease, neuraminidase and other glycosidic hydrolase treatments revealed the haemagglutinins to be protein, most likely glycoprotein, in nature ‐ not lipoprotein, lipid, glycolipid or nucleic acid. An.gambiae agglutinins were thermo‐labile >40 o C, affected by freezing and thawing treatments, and contained disulphide and hydrogen bonds on the basis of sensitivity following exposure to dithio‐threitol and urea respectively. Optimum haemagglutination depended generally on slightly acid to neutral pH conditions and agglutinin activity was Ca 2+ ion, albeit to a lesser extent Mg 2+ ion, dependent. The midgut extract agglutinin subunit molecule had a relative molecular weight (M r ) of 65kDa whilst that of haemolymph was 40kDa. This study presents the first report on selected physico‐chemical properties, the glycoproteinaceous nature and tentative subunit M r of mosquito midgut extract and haemolymph anti‐RBC agglutinin(s).