Abstract
Effects of wheat germ agglutinin on the coupled transports of sodium and potassium in reconstituted (Na,K)-ATPase liposomes.
Highlights
Transport was inhibited 51%. (Na,K)-ATPase activity of the liposomes was not inhibited under these conditions, suggesting partial uncoupling of transport from catalytic activity
We present data which show that interference with the glycoprotein subunit by means of wheat germ agglutinin binding inhibits transport of Na’ and K’ even though no change in total or transporting (Na,K)-ATPase activity can be observed
Previous work [17] showed that inhibition of (Na,K)-ATPase activity by wheat germ agglutinin occurred at higher ratios of wheat germ agglutinin to enzyme; 37% inhibition of (Na,K)-ATPase activity occurred at 500 pg/ml/ 100 pg of enzyme
Summary
Materials-Egg lecithin was purchased from EM Laboratories, Inc. Wheat germ agglutinin was routinely purchased from Calbiochem. Ion exchange resin was prepared before use by washing it with 2 volumes of 1 M Tris base with stirring for 15 min. It was rinsed ten times with 1 volume of deionized water. Activity-The liposomes were diluted 10 times with 1 mM Tris-EDTA (pH 7.0), and (Na,K)-ATPase activity was determined by incubating 0.1 ml for 5 min at 37°C with 0.4 ml of solution containing 150 mM NaCl, 25 mM KCl, 12.5 mM. (Na,K)-ATPase activity was measured in undiluted liposomes to determine whether the usual dilution step obscured an inhibition by wheat germ agglutinin. After 30 min at room temperature, the samples were read in a spectrophotometer at 660 nm
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
