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Recognition of hormones by membrane potential and circular dichroism of immobilized protein membranes
Author(s) -
Hara Mariko,
Higuchi Masahiro,
Minoura Norihiko,
Higuchi Akon
Publication year - 1997
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/(sici)1097-4628(19970711)65:2<251::aid-app5>3.0.co;2-n
Subject(s) - circular dichroism , membrane , chemistry , conformational change , albumin , biophysics , crystallography , biochemistry , biology
The shifts in membrane potential, caused by the injection of hormones into a permeation cell, were measured using immobilized (entrapped) serum albumin and γ‐globulin membranes. The effective fixed charge density was estimated to increase after the injection of estradiol and testosterone in both albumin and γ‐globulin membranes, while the charge density was estimated to decrease after the injection of progesterone in the γ‐globulin membranes. Because the change in the charge density originates from the conformational change of proteins in the membranes, the change in the circular dichroism induced by the hormones was measured in the membranes. The α‐helix content in both albumin and γ‐globulin membranes was found from the circular dichroism measurements to increase when estradiol and testosterone was bound to the proteins, while the α‐helix content in the albumin membrane decreased on the binding of progesterone. Some discrepancy was found between the conformational change of the proteins in the membranes detected by the membrane potential measurements and the circular dichroism measurements. This is explained by the fact that the circular dichroism measurements do not directly contribute to the change in the charge density induced by the binding of hormones to proteins in the membranes. © 1997 John Wiley & Sons, Inc. J Appl Polym Sci 65:251–259, 1997