Studies on Lectin From Glycine Max (L.) Merrill
C. Hemalatha, R. Dhamotharan1 and S. Murugesan2
1PG and Research Department of Plant Biology and Plant Biotechnology, Presidency College, Chennai - 600 005 (India). 2Unit of Algal Biotechnology and BionanoTechnology, PG and Research Department of Plant Biology and Plant Biotechnology, Pachaiyappa’s College, Chennai - 600 030 (India).
ABSTRACT: A plant lectin isolated in its pure state from the Indian of soya bean seeds produced single band in SDS–PAGE (30kDa) and one peak by gel filtration chromatography on Sephadex G-100, corresponding to 120 kDa. SBL is a glycoprotein bound with glucose and mannose (2 mol/mol of protein) and stabilized by 4 atoms of each of Ca2+ and Mn2+ per subunit. The soya bean lectin exhibited haemagglutinating activities in various degrees against human ABO type, rabbit and rat erythrocytes. Maximum activity was observed against rabbit and human AB blood groups. Among the various tested sugars, SBL agglutination was most inhibited by N-acetylgalactose. Hemagglutination was markedly affected by acidic pH, but was heat stable below 60°C for 30 min. The haemagglutinating activity of the soya bean lectin was inhibited by addition of Ca2+, Mg2+, Mn2+ and EDTA. SBL is rich in hydroxyl amino acids while totally lacking sulfur amino acids.
KEYWORDS: Soya bean lectin; Hemagglutination activity
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Copy the following to cite this article: Hemalatha C, Dhamotharan R, Murugesan S, Studies on Lectin From Glycine Max (L.) Merrill. Biosci Biotech Res Asia 2010;7(1) |
Copy the following to cite this URL: Hemalatha C, Dhamotharan R, Murugesan S, Studies on Lectin From Glycine Max (L.) Merrill. Biosci Biotech Res Asia 2010;7(1). Available from: https://www.biotech-asia.org/?p=9774 |