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Glutaraldehyde cross-linking of lectins to marker enzymes: Protection of binding site by specific sugars

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Title Glutaraldehyde cross-linking of lectins to marker enzymes: Protection of binding site by specific sugars
 
Creator Appukuttan, P S
Chacko, Balu K
Geetha, M
Annamma, K I
Mathai, Jaisy
 
Description 77-80
The role of bound specific sugars in protecting
the sugar binding activity of several galactose binding proteins during their covalent
conjugation to horse radish peroxidase by glutaraldehyde-mediated cross-linking
was examined by: a) affinity matrix binding of the conjugate, b) enzyme linked
lectin assay and c) hemagglutination assay. During conjugation using 1% glutaraldehyde,
protection of jack fruit (Artocarpus integrifolia) lectin
(jacalin) activity depended on concentration of specific sugar present during conjugation;
optimum protection was offered by 50 mM galactose. This indicated the
presence of one or more primary groups at the binding site or jacalin , which is
(are) essential for sugar binding. On the other hand, such essential amino group(s)
was not indicated at the sugar binding site of the peanut lectin, bovine heart
galectin or of the human serum anti α-galactoside antibody, since exclusion of sugar
during their conjugation to HRP did not diminish sugar

binding activity. The differential behavior
is discussed in the light of reported differences in sugar specificities. Results
indicated that sugar mediated blocking of active site may be used in characterization
of the latter in lectins.
 
Date 2013-07-16T07:01:21Z
2013-07-16T07:01:21Z
2000-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/19813
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.37(2) [April 2000]