M. Hara et al., RECOGNITION OF AMINO-ACIDS BY MEMBRANE-POTENTIAL AND CIRCULAR-DICHROISM OF IMMOBILIZED ALBUMIN MEMBRANES, Journal of applied polymer science, 58(11), 1995, pp. 2025-2032
The shifts in membrane potential, caused by the injection of some amin
o acids into a permeation cell, were measured using immobilized serum
albumin membranes at isoelectric points of the amino acids. The effect
ive fixed charge density was estimated to decrease after the injection
of alanine, phenylalanine, and tryptophan and to increase after the i
njection of serine. The change in the fixed charge density originated
from the conformational change of the immobilized albumin membranes in
duced by the binding between the albumin and amino acids in the membra
nes, since the conformational change of the immobilized albumin membra
nes induced by the binding of the amino acids to the serum albumin was
observed from circular dichroism measurements. There was found, howev
er, some discrepancy between the conformational change of the serum al
bumin in the albumin membranes detected by the membrane potential meas
urements and the circular dichroism measurements. This is explained by
the fact that the circular dichroism measurements detect the increase
or decrease in the alpha-helix, beta sheet, and random coil contents;
however, they do not always contribute to the detection of the change
in the charge density due to the presence of the amino acid in the al
bumin membranes. (C) 1995 John Wiley & Sons, Inc.