Dissociation, aggregation of sesame L- globulin in nonionic detergent solution.

Nonionic detergents Triton X-l00 and Brij 36T induce dissociation and aggregation
of the protein sesame Q-globulin above the critical micelle concentrations
(crnc) of the detergents. Spectrophotometric titration in Triton shows no change
in the pK1nl value of tile tyrosyl groups at 1 X 10-3 M detergent where both dissociation
and aggregation of the protein are observed. Fluorescence measurement
does not indicate any change in the environment of the tryptophan groups
of the protein in Brij. Viscosity measurements show no major conformational
change of the protein in the detergent solution. Binding measurements suggest
that perhaps micelles of the detergent predominantly bind to the protein. The
detergent micelles preferentially bind to the exposed hydrophobic surfaces of
the protein subunits. The association of the protein detergent complex through
electrostatic interaction is probably responsible for the formation of the aggregates.