Activity of Na /K -ATPase in model lipid membrane at air-water interface

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F19%3A73596141" target="_blank" >RIV/61989592:15110/19:73596141 - isvavai.cz</a>

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0013468619304669?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0013468619304669?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2019.03.063" target="_blank" >10.1016/j.electacta.2019.03.063</a>

Result language

angličtina

Original language name

Activity of Na /K -ATPase in model lipid membrane at air-water interface

Original language description

The Na+/K+-ATPase pump was reconstituted in proteoliposomes composed of DPPC: DPPE, which were then spread at the air-water interface using Langmuir technique. In the presence of the enzyme in the liposomes the resulting lipidic layer at the air-water interface became more liquid. The effect of Na+/K+-ATPase on the morphology of Langmuir lipidic layers was monitored by Brewster angle microscopy, which showed the formation of lattice-like structure in between round-shaped lipid domains. The presence of protein stabilized the DPPC:DPPE mixed monolayer at the air-water interface, which was revealed by surface pressure measurements in time and ascribed to hydrogen bond network formation between the protein and the lipids. The activity of the protein embedded in the lipidic Langmuir layer was measured using spectroscopy and voltammetry. Free phosphate released from ATP reacted with ammonium molybdate and the blue alpha-Keggin anion formed was detected spectrophotometrically at a wavelength of 710 nm. The results based on spectroscopic assay were complemented with electrochemical methods. The activity of the enzyme could by switched off using the inhibitor - ouabain. The Na+/K+-ATPase activity (2.62 nmol mg(-1) min(-1)) was similar to the activity of the protein solubilized using detergents (3.21 nmol mg(-1) min(-1)). The slightly lower activity was ascribed to the defined orientation of the embedded protein molecules with respect to the air-water interface needed for its activity at the air-water interface. (

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

ELECTROCHIMICA ACTA

ISSN

0013-4686

e-ISSN

—

Volume of the periodical

305

Issue of the periodical within the volume

may

Country of publishing house

GB - UNITED KINGDOM

Number of pages

8

Pages from-to

204-211

UT code for WoS article

000462774000022

EID of the result in the Scopus database

2-s2.0-85063250177