Lectin binding to complex carbohydrate at the interface: a study by resonance energy transfer.
Indian J Biochem Biophys
;
1992 Jun; 29(3): 262-5
Article
in English
| IMSEAR
| ID: sea-27257
ABSTRACT
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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Oligosaccharides
/
Phosphatidylethanolamines
/
Ricin
/
Spectrometry, Fluorescence
/
Carbohydrates
/
Dimyristoylphosphatidylcholine
/
Energy Transfer
/
Galactose
/
Liposomes
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1992
Type:
Article
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