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Recognition of amino acids by membrane potential and circular dichroism of immobilized albumin membranes
Author(s) -
Hara Mariko,
Higuchi Masahiro,
Minoura Norihiko,
Higuchi Akon
Publication year - 1995
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.1995.070581113
Subject(s) - circular dichroism , membrane , albumin , chemistry , amino acid , isoelectric point , conformational change , tryptophan , random coil , isoelectric focusing , serum albumin , chromatography , biochemistry , enzyme
The shifts in membrane potential, caused by the injection of some amino acids into a permeation cell, were measured using immobilized serum albumin membranes at isoelectric points of the amino acids. The effective fixed charge density was estimated to decrease after the injection of alamine, phenylalanine, and tryptophan and to increase after the injection of serine. The change in the fixed charge density originated from the conformational change of the immobilized albumin membranes induced by the binding between the albumin and amino acids in the membranes, since the conformational change of the immobilized albumin membranes induced by the binding of the amino acids to the serum albumin was observed from circular dichroism measurements. There was found, however, some discrepancy between the conformational change of the serum albumin in the albumin membranes detected by the membrane potential measurements and the circular dichroism measurements. This is explained by the fact that the circular dichroism measurements detect the increase or decrease in the α‐helix, β 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 albumin membranes. © 1995 John Wiley & Sons, Inc.