Isolation and characterization of a lectin from the visceral region of the golden snail, Pomacea sp.
1994
Lacsamana M.S. | Merca F.E.
A lectin with mitogenic activity was isolated from the visceral region of the golden snail, Pomacea sp., by extraction with phosphate buffer (pH 7.2). The lectin was purified by pH adjustment, ammonium sulfate precipitation and gel filtration on Sephadex G-200. Mitogenic activity was assayed morphologically in terms of the induction of lymphoblasts in cultures containing the purified lectin and lymphocytes from fresh human blood, and comparison with a negative control and a positive control which contained the Phaseolus vulgaris lectin. The Pomacea sp. lectin was found to be both non-blood type and non-blood group specific because it agglutinated the erythrocytes from human blood types A, B, O, and AB, and those from carabao, cattle, and goat. Treatment of the erythrocytes with trypsin had a positive effect on the agglutination behavior of the lectin. The carbohydrates-binding specificity of the lectin was not directed towards any of the sugars tested. The purified lectin was disclosed to be a glycoprotein containing 11.4 percent total sugars. The sugar residues were identified by high performance liquid chromatography (HPLC) as galactose and mannose. High amounts of glutamic acid, leucine, aspartic acid and arginine were present in the protein portion of the lectin. SDS-PAGE analysis of the purified lectin showed that it is composed of four different sub-units of molecular masses 120 KD, 115 KD, 105 KD, and 100 KD.
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