Abstract
A lectin specific for glucuronic acid and galacturonic acid has been isolated from seeds of the French bean Phaseolus vulgaris using a procedure that involved affinity chromatography on Affi-gel blue gel, fast protein liquid chromatography (FPLC)-ion exchange chromatography on Mono S, and FPLC-gel filtration on Superdex 200. The lectin was comprised of two 32-kDa subunits with substantial N-terminal sequence similarity to other Phaseolus lectins. The hemagglutinating activity of the lectin was stable within the pH range of 1-13 and the temperature range of 10-60 C. The lectin neither exhibited any antiproliferative activity against tumor cells nor stimulated nitric oxide production by murine peritoneal macrophages at doses as high as 1mM , The lectin failed to evoke any mitogenic response from murine splenocytes as measured by [3H-methyl]-thymidine incorporation and did not inhibit the activity of HIV-1 reverse transcriptase. The lectin had no antifungal activity.
Keywords: Lectin, Indian cultivar of French bean, seeds, isolation, thermostable, glucuronic acid and galacturonic acid specific
Protein & Peptide Letters
Title: Purification and Characterization of a Lectin from the Indian Cultivar of French Bean Seeds
Volume: 17 Issue: 2
Author(s): A. Sharma, Jack H. Wong, Peng Lin, Y. S. Chan and T. B. Ng
Affiliation:
Keywords: Lectin, Indian cultivar of French bean, seeds, isolation, thermostable, glucuronic acid and galacturonic acid specific
Abstract: A lectin specific for glucuronic acid and galacturonic acid has been isolated from seeds of the French bean Phaseolus vulgaris using a procedure that involved affinity chromatography on Affi-gel blue gel, fast protein liquid chromatography (FPLC)-ion exchange chromatography on Mono S, and FPLC-gel filtration on Superdex 200. The lectin was comprised of two 32-kDa subunits with substantial N-terminal sequence similarity to other Phaseolus lectins. The hemagglutinating activity of the lectin was stable within the pH range of 1-13 and the temperature range of 10-60 C. The lectin neither exhibited any antiproliferative activity against tumor cells nor stimulated nitric oxide production by murine peritoneal macrophages at doses as high as 1mM , The lectin failed to evoke any mitogenic response from murine splenocytes as measured by [3H-methyl]-thymidine incorporation and did not inhibit the activity of HIV-1 reverse transcriptase. The lectin had no antifungal activity.
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Cite this article as:
Sharma A., Wong H. Jack, Lin Peng, Chan S. Y. and Ng B. T., Purification and Characterization of a Lectin from the Indian Cultivar of French Bean Seeds, Protein & Peptide Letters 2010; 17 (2) . https://dx.doi.org/10.2174/092986610790226067
DOI https://dx.doi.org/10.2174/092986610790226067 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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