Abstract
A Archidendron jiringa Nielsen lectin was purified by aqueous extraction, 90% ammonium sulphate precipitation and concanavalinA-Sepharose 4B affinity chromatography. Its specific activity was of 88.3×102 hemagglutination unit/mg protein for a yield of 51.6% total protein. The molecular weight is of 35.7kDa. It has hemagglutinating activity against human blood group, rabbit, mouse, rat, guinea pig, geese and sheep erythrocytes. The hemagglutination activity of lectin was relatively insensitive to acidic pH above 2, had an optimal activity at pH 8, and stable below 45°C for 30min. The activity was stimulated by Ca2+, Mg2+ and Mn2+. The internal sequence indicated similarity with legume lectin family. Moreover, even at low concentrations antifungal activity was observed against Exserohilum turcicum, Fusarium oxysporum and Colletotrichum cassiicola. The minimal inhibitory concentrations were 0.227, 0.0567 and 0.0567mg/ml for Bacillus subtilis, Staphylococcus aureus, and Candida albicans, respectively.
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