A Novel Antiproliferative and Antifungal Lectin from Amaranthus viridis Linn Seeds

Authors: Kaur, Navjot; Dhuna, Vikram; Kamboj, Sukhdev Singh; Agrewala, Javed N; Singh, Jatinder

Source: Protein and Peptide Letters, Volume 13, Number 9, September 2006 , pp. 897-905(9)

Publisher: Bentham Science Publishers

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A lectin from the seeds of Amaranthus viridis Linn has been purified by affinity chromatography on asialofetuin- linked amino activated silica. Amaranthus viridis lectin (AVL) has a native molecular mass of 67 kDa. It is a homodimer composed of two 36.6 kDa subunits. The lectin gave a single band in non-denaturing PAGE at pH 4.5 and pH 8.3 and a single peak on HPLC size exclusion and cation exchange columns. The purified lectin was specific for both Tantigen and N-acetyl-D-lactosamine, markers for various carcinomas, in addition to N-acetyl-D-galactosamine, asialofetuin and fetuin. This lectin reacted strongly with red blood cells (RBCs) from human ABO blood groups and rat. It also reacted with rabbit, sheep, goat and guinea pig RBCs. The lectin is a glycoprotein having no metal ion requirement for its activity. Denaturing agents such as urea, thiourea and guanidine-HCl had no effect on its activity when treated for 15 minutes. AVL showed significant antiproliferative activity towards HB98 and P388D1 murine cancer cell lines. It also exerted antifungal activity against phytopathogenic fungi Botrytis cincerea and Fusarium oxysporum but not against Rhizoctonia solani, Trichoderma reesei, Alternaria solani and Fusarium graminearum.

Keywords: Affinity purification; Amaranthus viridis; N-acetyl-D-lactosamine; T-antigen; amaranthaceae; asialofetuin; lectin

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606778256153

Affiliations: Department of Molecular Biology and Biochemistry, Guru Nanak Dev University, Amritsar 143 005, India.

Publication date: September 1, 2006

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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