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A glucuronic acid binding leguminous lectin with mitogenic activity toward mouse splenocytes
Yau Sang Chan1, Jack Ho Wong, Tzi Bun Ng
1School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China.
Protein and Peptide Letters
|November 9, 2010
Summary
A French bean lectin was purified and characterized for its hemagglutinating and mitogenic activities. Glucuronic acid inhibited these activities, and the lectin showed no antiproliferative effects on cancer cells.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- Lectins are proteins known for their carbohydrate-binding properties.
- Plant lectins, such as those from Phaseolus vulgaris (French bean), are extensively studied for their biological activities.
Purpose of the Study:
- To purify and characterize a lectin from French bean seeds.
- To investigate the hemagglutinating, mitogenic, and antiproliferative activities of the purified lectin.
Main Methods:
- Purification using Q-Sepharose, Affi-gel blue gel, Mono S, and Superdex 75 chromatography.
- Hemagglutinating activity assays across a range of pH and temperatures.
- Mitogenic activity assays using murine splenocytes.
- Antiproliferative assays against cancer cell lines (HepG2, MCF7, CNE).
Main Results:
- A dimeric 64-kDa lectin was purified, showing a single 32-kDa band under SDS-PAGE.
- The lectin exhibited full hemagglutinating activity between pH 3-11 and temperatures of 20-60 °C.
- Glucuronic acid inhibited hemagglutinating and mitogenic activities.
- The lectin demonstrated maximum mitogenic activity at 0.488 µM and no antiproliferative activity against tested cancer cells.
Conclusions:
- The purified French bean lectin possesses significant hemagglutinating and mitogenic properties.
- Its activity is modulated by pH, temperature, and specifically inhibited by glucuronic acid.
- The lectin lacks antiproliferative effects on tested cancer cell lines and anti-HIV reverse transcriptase activity.
