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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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. (

Název v anglickém jazyce

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

Popis výsledku anglicky

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. (

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

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

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

ELECTROCHIMICA ACTA

ISSN

0013-4686

e-ISSN

—

Svazek periodika

305

Číslo periodika v rámci svazku

may

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

204-211

Kód UT WoS článku

000462774000022

EID výsledku v databázi Scopus

2-s2.0-85063250177