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Submitted: 16 May 2007 Modified: 30 August 2018
HERDIN Record #: PCHRDPC060505

Purification and characterization of plant lectins as potential source of hemagglutinin and anti-cancer drug.

 Dungca, Julieta Z,
 Panlasigui, Priscill,
 Cruz, Rogelio S

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Twenty plant samples collected from Laiya, San Juan, Batangas were used in the study. Lectins, the carbohydrate binding proteins from indigenous plants, were extracted and homogenized from the different plant samples using phosphate buffer saline (PBS) followed by protein precipitation using saturated ammonium sulfate (SAS). The protein suspension was dialyzed against phosphate buffer saline (PBS) for five days. The dialysate was allowed to pass through Sephadex G-50 (size exclusion chromatography) to collect the different protein fractions. Each fraction was read spectrophotometrically at 300 nanometer to determine protein peaks. The study confirmed the presence of protein in seven plant samples, which gave a significant spectrophotometric reading comparable to the lectin standard at 0.300 - 2.500 absorbance. The hemagglutinating property of plant lectin was analyzed in V-shaped microtiter plate using crude protein extract. The positive red blood cell agglutination was indicated by a mat-like appearance (carpeting) at the bottom of the well. However, when the entire solution exhibits a pinkish color, hemolysis occurs, suggesting that the crude extract has a hemolytic property. (Author)

Publication Type
CEU Graduate Studies S & T Res Symposium and Poste
September 8-11, 2001
LocationLocation CodeAvailable FormatAvailability
Philippine Council for Health Research and Development Library Abstract Print Format (Request Document)