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
Protein & Peptide Letters
Title:Purification and Characterization of a Novel Anti-Proliferative Lectin from Morus alba L. Leaves
Volume: 19 Issue: 8
Author(s): Mundekkad Deepa and Sulochana Priya
Affiliation:
Keywords: Mulberry leaf lectin, immobilized metal affinity chromatography, convective interaction media, haemagglutination, antiproliferative, cytotoxicity, Lectins, oligosaccharides, carbohydrate binding specificity, inter-residue glycosidic linkages
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.
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Cite this article as:
Deepa Mundekkad and Priya Sulochana, Purification and Characterization of a Novel Anti-Proliferative Lectin from Morus alba L. Leaves, Protein & Peptide Letters 2012; 19(8) . https://dx.doi.org/10.2174/092986612801619516
DOI https://dx.doi.org/10.2174/092986612801619516 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |

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