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Abstract

A lectin curcin was isolated from mature seeds of Jatropha curcas L. Seeds were collected locally and purified by affinity chromatography on guar gum column. The lectin content was found to be 1.3 mg/ml. Curcin agglutinated B +ve human RBC type showing galactose and Ngalactosylamine specificity. Galactose sugar was found to be the most potent inhibitor of curcin hemagglutinating activity (minimum inhibitory concentration (MIC) ≤ 50 mM). The lectin was a glycoprotein with a neutral carbohydrate content of 0.26µg/ml. The molecular mass of protein was found to be 28 kDa similar to previous reports of separation by SDS-PAGE. Curcin was stable at pH range from 4-10 while for temperature range it was stable from 10 ºC to 80 ºC for 30 min. Alignment with other lectin proteins by BLAST tool resulted into its similarity to 17 entries with 10 proteins with 100% query coverage but only RIP (Ribosome Inhibiting Protein domain) was visible in search results while carbohydrate binding domain was absent. INTRODUCTION: Jatropha curcas L. is drought resistant, a multipurpose perennial plant belonging to Euphorbiaceae family. All parts of Jatropha plant viz. leaf, fruits, latex, and bark have been used in different aliments as traditional medicine in many countries 1. The plant exhibits antibacterial, antifungal and anticancer properties 2-4. Nowadays Jatropha is gaining importance for its oil which is regarded as potential fuel substitute 5. In addition to oil, it also provides a high protein for which it is a supplement in animal feed and manure 6. Along with all these potential applications of Jatropha in biopharmaceuticals and bioenergy production, the seeds of Jatropha curcas are found to be toxic to humans and animals.