AFFINITY CHROMATOGRAPHY PURIFICATION AND PARTIAL CHARACTERISATION OF D-GALACTOSE BINDING LECTIN FROM SEEDS OF JATROPHA CURCAS L.
AbstractA 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 N-galactosylamine 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.
Article Information
54
2487-2491
583
850
English
IJPSR
R. M. Phadke and K. Pai *
Department of Zoology, Savtribai Phule Pune University, Ganeshkhind, Pune, Maharashtra, India.
drkalpanapi@gmail.com
06 September 2018
28 December 2018
20 January 2019
10.13040/IJPSR.0975-8232.10(5).2487-91
01 May 2019
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