Purification of lectin from mulberry leaves
1995
Sunanta Ratanapo (Kasetsart Univ., Bangkok (Thailand). Faculty of Science. Dept. of Biochemistry)
Lectins are proteins or glycoproteins with multiple carbohydrate-binding sites. They are also called agglutinin because of their abilities to agglutinate various animal erythrocytes. Hundreds of lectins are found in plants, but few bind to sialic acids. The presence of lectins in mulberry leaves was established in 20 local mulberry cultivars. Four sialic acid specific lectins, ML-1, ML-2a, ML-2b and ML-3 were purified from leaves of the mulberry on N-acetylgalactos-amine agarose and gel filtration on Sephacryl S-200. The hemagglutination inhibition study cleary suggested that the four lectins were specific to N-glycolyl-neuraminic acid. Their activities were also inhibited by high concentrations of N-acetylgalactosamine or galactose. On Sephacryl S-200, the native molecular weight of ML-1 was found to be higher than 669,000 and of ML-3 was found to be lower than 13,700. ML-2a and ML-2b were coeluted on the Sephacryl S-200, having the native molecular weight of 44,000. The lectins ML-2a and ML-2b were separated by FPLC on an anion-exchange column, Mono Q. Both ML-2a and ML-2b were found to be heat-libile glycoproteins containing 1.93 percent and 54.78 percent neutral sugars, respectively. By isochromatofocusing chromatography, pI values of the both lectins were found to be 6.75 and 4.5, respectively. No calcium ion was required for their binding activities.
Show more [+] Less [-]AGROVOC Keywords
Bibliographic information
This bibliographic record has been provided by Thai National AGRIS Centre, Kasetsart University
