ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Studies on the interaction of concanavalin A with glycoproteins

Surolia, A and Bishayee, S and Ahmad, A and Balasubramanian, KA (1975) Studies on the interaction of concanavalin A with glycoproteins. In: Adv Exp Med Biol, 55 . pp. 95-115.

Full text not available from this repository. (Request a copy)
Official URL: http://www.ncbi.nlm.nih.gov/pubmed/239536


Lectins (phytohaemagglutinin) are known to have the unique property of binding with certain specific sugars, polysaccharides and glycoproteins. Although the kinetics of interaction between lectins and sugar have been extensively studied, the binding characteristics of the lectins with various glycoproteins are not well understood. In this laboratory a systematic study has been initiated in relation to the interaction of lectins with glycoproteins. Concanavalin A is known to bind alpha-glucosides, mannosides and biopolymers having these sugar configurations. A galactose binding protein from caster bean has been purified to homogeneity and was found to contain mannose. This lectin was used as the source of glycoprotein for studying its interaction with concanavalin A. This study showed that the interaction is temperature dependent and the dissociation is time and alpha-methyl glucoside concentration dependent. This has led to speculate a model for cell-lectin interaction. Using concanavalin A it has been shown that all the lysosomal enzymes from brain studied were glycoprotein in nature. Moreover, using Sepharose-bound concanavalin A it has been possible to devise a method by which these lysosomal enzymes could be purified considerably. With the knowledge that the interaction between lectin and glycoprotein is not only dependent on the specific sugar present in the glycoprotein, but also on the nature of the glycoprotein it was possible to develop a novel method for immobilizing various glycoprotein enzymes, such as arylsulphatase A, hyaluronidase and glucose oxidase.

Item Type: Journal Article
Publication: Adv Exp Med Biol
Publisher: National Center for Biotechnology Information
Additional Information: Copyright of this article belongs to National Center for Biotechnology Information.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 18 May 2010 09:42
Last Modified: 18 May 2010 09:42
URI: http://eprints.iisc.ac.in/id/eprint/27563

Actions (login required)

View Item View Item