Articles written in Journal of Biosciences
Volume 4 Issue 2 June 1982 pp 133-138
The acidic α-mannosidase was purified 4400-fold by affinity chromatography on Concavalin A-Sepharose and heat treatment at 65‡C in the presence of 1 mM zinc ion. The enzyme did not resolve into multiple forms as in the case of enzymes from human liver and human kidney. The pH optimum of the enzyme was 4.2 in citrate-phosphate buffer. The Km value for p-nitrophenyl-α-D-mannose was 1.9 mM. The molecular weight of the enzyme determined by gel filtration was 300,000. The enzyme contained 10.6% neutral sugars.
Volume 4 Issue 3 September 1982 pp 257-261
An α-D-galactose-specific lectin from the seeds of jack fruit (
Volume 5 Issue S1 December 1983 pp 131-135
N-Acetyl-D-galactosamine in β-linkage being ubiquitous in cell surface glycoproteins, their interaction with lectins specific for this sugar moiety may be a significant event in cell adhesion phenomena. This article discusses the common β-N-acetyl galactosamine-specific lectins, with particular stress on the lectin from winged beans (
Volume 7 Issue 1 March 1985 pp 7-14
The effect of chemical modification of amino acid residues essential for sugar binding in the α-D-galactoside specific jack fruit (
Volume 11 Issue 1-4 March 1987 pp 41-46
Lectins, the divalent or polyvalent (glyco) proteins of non-immune origin of the cells agglutinate cells or other materials, that display more than one saccharide of sufficient complementarity. Lectins considered ‘identical’ in terms of mono-and disaccharide specificity can be differentiated by their ability to recognise the fine differences in more complex structures. The present review discusses the interaction of lectins with various oligosaccharides and their resultant separations due to structural variations.
Volume 11 Issue 1-4 March 1987 pp 331-338
The galactose-binding lectin of human Placenta has been Purified to homogeneity by affinity chromatograPhy on asialo-fetuin column. The Protein, extractable from the tissue only with lactose is aPParently membrane-bound. Molecular weight determination of native Protein and subunit indicated a dimer of l3.4 kDa subunits. Inhibition of haemagglutination with various saccharides indicate that thiodigalactoside is the best inhibitor followed by lactose. However,
Volume 12 Issue 1 March 1987 pp 61-69
An acid α-galactosidase from the seeds of the jack fruit seed (