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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Purification and Characterization of a Novel Anti-Proliferative Lectin from Morus alba L. Leaves

Author(s): Mundekkad Deepa and Sulochana Priya

Volume 19, Issue 8, 2012

Page: [839 - 845] Pages: 7

DOI: 10.2174/092986612801619516

Price: $65

Abstract

A novel anti-proliferative lectin was purified from Morus alba L. (Mulberry) leaves by a two step chromatographic procedure namely, immobilized metal ion affinity chromatography (IMAC) and convective interaction media (CIM) based anion exchange chromatography. The purified mulberry leaf lectin (MLL) was specific to galactose, galactosamine and N-acetyl galactosamine (GalNAc). MLL was homogenous with a molecular weight of ~56kDa in silver stained SDS-PAGE. The lectin showed RBC agglutination activity up to 40°C and was independent of pH above pH 6. Haemagglutination activity of purified MLL was not dependent on any metal ions. However, with high concentration of trivalent metal ions, Fe3+ and Al3+ and the divalent metal ion Fe2+, a three fold increase in agglutination activity was observed. The purified MLL showed an anti-proliferative activity towards human breast cancer cells (MCF-7) and colon cancer cells (HCT-15) with a higher potency towards MCF-7 cells. This is the first report on the anti-proliferative activity of a GalNAc specific lectin from M. alba.

Keywords: Mulberry leaf lectin, immobilized metal affinity chromatography, convective interaction media, haemagglutination, antiproliferative, cytotoxicity, Lectins, oligosaccharides, carbohydrate binding specificity, inter-residue glycosidic linkages


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