A lectin has been isolated from seeds of the Phaseolus vulgaris cv. “Anasazi beans” 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 30-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 1–14 and the temperature range of 0–80°C. The lectin potently suppressed proliferation of MCF-7 (breast cancer) cells with an IC50 of 1.3 μM, and inhibited the activity of HIV-1 reverse transcriptase with an IC50 of 7.6 μM. The lectin evoked a mitogenic response from murine splenocytes as evidenced by an increase in [3H-methyl]-thymidine incorporation. The lectin had no antifungal activity. It did not stimulate nitric oxide production by murine peritoneal macrophages. Chemical modification results indicated that tryptophan was crucial for the hemagglutinating activity of the lectin.
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 degrees 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 [(3)H-methyl]-thymidine incorporation and did not inhibit the activity of HIV-1 reverse transcriptase. The lectin had no antifungal activity.
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