Chakrabarti, A and Podder, SK (1992) Lectin binding to complex carbohydrate at the interface: a study by resonance energy transfer. In: Indian Journal of Biochemistry & Biophysics, 29 (3). pp. 262-265.Full text not available from this repository.
The binding affinity of the oligosaccharide moiety of a neutral glycosphingolipid, asialoGM1, towards Ricinus communis agglutinin (RCAI) was determined for the first time by fluorescence resonance energy transfer (RET). The asialoGM1 was incorporated into a phospholipid (DMPC) vesicle doped with dansylated DPPE and then titrated with an increasing amount of the galactose specific RCAI. The efficiency of RET was determined by a saturable increase in the quenching of 'donor' fluorescence, i.e. the 'trp' residue of RCAI, due to the energy transfer from the 'acceptor' dansyl group on the surface of the vesicle. The apparent binding constant was found to be in the range of 10(5)-10(6) M-1 at 27 degrees C.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National Institute of Science Communication and Information Resources.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||05 May 2011 06:45|
|Last Modified:||05 May 2011 06:45|
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