PMID: 1259Nov 15, 1975

Factors affecting the molecular structure and the agglutinating ability of concanavalin A and other lectins

European Journal of Biochemistry
M Huet

Abstract

Ultracentrifugation analyses were performed on lectins under varying conditions of pH, ionic strength and temperature. It has been demonstrated that the phytohemagglutinin from Phaseolus vulgaris, the wheat germ agglutinin and the soybean agglutinin are stable when these parameters are varied, whereas the concanavalin A molecule exhibits a striking reversible dimer-tetramer transition with variation in pH (from 6.0 to 7.2) and temperature (from 4 degrees up to 37 degrees C). It has also been demonstrated that, in agglutination experiments undertaken at different temperatures, cells do eventually aggregate with the first three lectins provided that incubation time is sufficient, whereas the concanavalin-A-induced agglutination was previously found to be temperature-sensitive. These results strongly suggest that the effect of temperature on agglutination by lectins may essentially be due to a structural transition of the lectin itself and nott only to modification of cell surface properties.

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Citations

Nov 30, 1995·European Journal of Pharmacology·K T YueD R Hampson
Aug 6, 2010·Analytical Chemistry·Yongdong Wang, Ming Gu
Jun 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·K R OldenburgM A Gallop
Nov 1, 1987·Revista Do Instituto De Medicina Tropical De São Paulo·I T NojimotoM E Camargo
Nov 29, 2019·Journal of Materials Chemistry. B, Materials for Biology and Medicine·Panagiotis G GeorgiouMatthew I Gibson

Related Concepts

Agglutination
Concanavalin A
Hydrogen-Ion Concentration
Methylmannosides
Osmolality
Plasma Protein Binding Capacity
Protein Conformation
Animal Lectins

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Antibodies: Agglutination

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