Related Experiment Video
Updated: Aug 4, 2026
Detection of Detergent-sensitive Interactions Between Membrane Proteins
Published on: March 7, 2018
Effects of detergent on the binding of solubilized sodium channels to immobilized wheat germ agglutinin: structural
1Department of Physiology and Biophysics, New York University Medical Center, New York 10016.
Abstract:
The binding of the solubilized voltage-dependent sodium channel from rat brain to immobilized wheat germ agglutinin (WGA) is detergent-dependent. When solubilized in sodium cholate, only 11% of total recovered channels bound to a WGA-Sepharose column. When solubilized in Triton X-100 or CHAPS, however, 80% and 60% could bind, respectively. The effect of cholate on sodium channel binding is relatively specific: the major rat brain glycoproteins which bind to immobilized WGA are roughly the same in either Triton or cholate, as analyzed by SDS gel electrophoresis. The structural implications for the channel are discussed.
More Related Videos
Related Concept Videos
01:18Detergent Purification of Membrane Proteins
01:27SDS-PAGE
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...