caa a22 4500 465826679 CHVBK 20180323112151.0 cr unu---uuuuu 170327e19900701xx s 000 0 eng 10.1007/BF01075675 doi (NATIONALLICENCE)springer-10.1007/BF01075675 Pressure adaptation of teleost gill Na+/K+-adenosine triphosphatase: role of the lipid and protein moieties [Elektronische Daten] [Allen Gibbs, George Somero] Summary: The effects of temperature and pressure on Na+/K+-adenosine triphosphatases (Na+/K+-ATPases) from gills of marine teleost fishes were examined over a range of temperatures (10-25°C) and pressures (1-680 atm). The relationship between gill membrane fluidity and Na+/K+-ATPase activity was studied using the fluorescent probe 1,6-diphenyl-1,3,5-hexatriene (DPH). The increase in temperature required to offset the membrane ordering effects of high pressure was 0.015-0.025°C·atm-1, the same coefficient that applied to Na+/K+-ATPase activities. Thus, temperature-pressure combinations yielding the same Na+/K+-ATPase activity also gave similar estimates of membrane fluidity. Substituion of endogenous lipids with lipids of different composition altered the pressure responses of Na+/K+-ATPase. Na+/K+-adenosine triphosphatase became more sensitive to pressure in the presence of chicken egg phosphatidylcholine, but phospholipids isolated from fish gills reduced the inhibition by pressure of Na+/K+-ATPase. Cholesterol increased enzyme pressure sensitivity. Membrane fluidity and pressure sensitivity of Na+/K+-ATPase were correlated, but the effects of pressure also dependent on the source of the enzyme. Our results suggest that pressure adaptation of Na+/K+-ATPase is the result of both changes in the primary structure of the protein and homeoviscous adaptation of the lipid environment. Springer-Verlag, 1990 Homeoviscous adaptation nationallicence Lipid substitution nationallicence Membrane fluidity nationallicence Na+/K+-ATPase nationallicence Pressure nationallicence EDTA nationallicence DPH : 1,6-diphenyl-1,3,5-hexatriene nationallicence PC : phosphatidylcholine nationallicence PL : phospholipid nationallicence SDH : succinate dehydrogenase nationallicence Gibbs Allen Marine Biology Research Division, A-002, Scripps Instituion of Oceanography, University of California, 92093, San Diego, La Jolla, CA, USA aut Somero George Marine Biology Research Division, A-002, Scripps Instituion of Oceanography, University of California, 92093, San Diego, La Jolla, CA, USA aut Journal of Comparative Physiology B Springer-Verlag 160/4(1990-07-01), 431-439 0174-1578 160:4<431 1990 160 360 https://doi.org/10.1007/BF01075675 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF01075675 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Gibbs Allen Marine Biology Research Division, A-002, Scripps Instituion of Oceanography, University of California, 92093, San Diego, La Jolla, CA, USA aut NATIONALLICENCE 700 1- Somero George Marine Biology Research Division, A-002, Scripps Instituion of Oceanography, University of California, 92093, San Diego, La Jolla, CA, USA aut NATIONALLICENCE 773 0- Journal of Comparative Physiology B Springer-Verlag 160/4(1990-07-01), 431-439 0174-1578 160:4<431 1990 160 360 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer