International Journal of  Applied Bioresearch (IJAB)

ISSN 2250 - 2033 (Print); e -ISSN: 2250 - 2041 (Online)

New Lectin from Bryophyllum mortagei

P. Rama Devi, G.R. Learnal Sudhakar and G.Lakshmanan

Volume No. 8                                                                                              15,June 2012

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Abstract

A 210kDa L- rhamnose-binding lectin was isolated from the leaf of Bryophyllum mortagei by gel filtration on Sephadex G-75 column. Bryophyllum mortagei lectin (designated as BmL) is a 160kDa protein consisting of 36kDa subunits linked by non-covalent bonds as determined by SDS-PAGE electrophoresis in the presence of 2-mercaptoethanol. The lectin exhibited strong heamagglutinating activity towards rabbit erythrocytes. Trypsinated rabbit RBC increased and papain treated decreased the activity. Its heamagglutinating activity was stable in pH range of 7.0–10.0 and temperature was stable up to 60o C and the heamagglutinating activity was lost at 80o C. The metal ions did not enhance the lectin activity. Keywords: Bryophyllum mortagei (BmL), L- rhamnose, Sephadex G-75, Red blood cells (RBC).