English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

Na+, K+-dependent ATPase is an intrinsic enzyme embeded in the plasma membranes. The function of the enzyme is to replace intracellular sodium ions with extracellular potassium ions using the free energy of ATP hydrolysis in animal cells. In this paper, the effect of dibucaine (D) on the enzyme was investigated. The p-NPPase and Na+, K+-ATPase activities of the enzyme were measured in various concentrations of D. The apparent affinities of the D-treated enzyme for ATP, Na+, Mg2+ and K+ were examined. Low concentrations of D inhibited the enzyme slightly, whereas higher concentrations inhibited the enzyme greatly. The apparent affinities of the enzyme for ATP, Mg2+ and K+ were changed by the treatment with high concentrations of D. The apparent affinity for K+ was only slightly changed by the treatment with low concentrations of D. The enzyme treated with high concentrations of D in the presence of K+ was shown to be slightly inhibited with the increase in the apparent affinity for ATP. The results were as follows : D is bound to the enzyme and causes a decrease in the p-NPPase and Na+, K+-ATPase activities. At least two apparently different D-binding sites, high and low exist. K+ ihibites D-binding to low-affinity sites. The inhibitory effects of D is possibly due to interference with the interaction between the enzyme protein and the phospholipids.

Dibucaine induced changes in Na+, K+-ATP ase: Influence on the interaction between substrates and enzyme.