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Purification and Characterization of Lectins from Jute ( Chorchorus olitorius ) Leaves
Author(s) -
Khan M. M. H.,
Rahman A. T. M. Mijanur,
Uddin Md. Salim,
Khatun Shahanaz,
Pervin F.,
Absar N.
Publication year - 2008
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.200800173
Subject(s) - chemistry , lectin , sephadex , chromatography , size exclusion chromatography , urea , ammonium sulfate , agglutination (biology) , polyacrylamide gel electrophoresis , sugar , ammonium , affinity chromatography , biochemistry , antibody , organic chemistry , enzyme , immunology , biology
Three lectins were isolated from an extract of jute leaves ( Chorchorus olitorius ) and purified by gel filtration on Sephadex G‐50 of the 100% ammonium sulfate saturated crude extract, followed by ion‐exchange chromatography on DEAE‐cellulose were designated as JLL‐1, JLL‐2 and JLL‐3. All the lectins were homogeneous as judged by SDS‐polyacrylamide slab gel electrophoresis and gave single bands. The molecular weights of the three lectins were estimated by the same method were 35000, 38000 and 42000, respectively. The lectins specifically agglutinated rat red blood cells. The agglutination of JLL‐1 was inhibited by D‐mannose/D‐glucose and their derivatives, whereas D‐galactose was found to be the potent inhibitor for the agglutination of JLL‐2 and JLL‐3. The lectins were glycoprotein in nature with a neutral sugar content of 1.3%, 1.2% and 0.8% for JLL‐1, JLL‐2 and JLL‐3, respectively. The hemagglutinating activity of JLL‐2 was also investigated after the treatment of physico‐chemical agents. The lectin showed maximum activity between the range of pH 7.2–8.0 and the range of temperature of 20‐30 °C. The activity of lectin decreased after treatment with a higher concentration of acetic acid and urea. In the presence EDTA the activity was inhibited while the presence of Ca +2 , Mn +2 and K + increased the activity of the lectin moderately.