Purification and characterization of a novel anti-proliferative lectin from Morus alba L. leaves.

Protein Pept Lett

Centre for Bio-Separation Technology (CBST), VIT University, Vellore, Tamil Nadu, 632014, India.

Published: August 2012

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.

Download full-text PDF

Source
http://dx.doi.org/10.2174/092986612801619516DOI Listing

Publication Analysis

Top Keywords

novel anti-proliferative
8
anti-proliferative lectin
8
morus alba
8
metal ion
8
agglutination activity
8
purified mll
8
metal ions
8
anti-proliferative activity
8
cancer cells
8
lectin
5

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!