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Journal of Experimental Biology, Vol 143, Issue 1 475-492, Copyright © 1989 by Company of Biologists
JOURNAL ARTICLES |
A Gibbs and GN Somero
Marine Biology Research Division, Scripps Institution of Oceanography, University of California, San Diego, La Jolla 92093.
The effects of pressure and temperature on an integral membrane protein, Na+/K+-adenosine triphosphatase (Na+/K+-ATPase), were studied in fish gill membrane preparations from shallow- and deep-living marine teleosts. The inhibition by pressure of maximal velocity of the enzyme is nonlinear, increasing at higher pressures. Na+/K+-ATPases from deep-sea fish were less inhibited by pressure than those of shallow-living species. Habitat temperature also affected the pressure response of the enzyme. As a function of physiological pressure and temperature, the order of increasing pressure-sensitivity was cold, deep-sea less than warm, deep-sea (hydrothermal vents) less than polar = shallow and mid-depth, cold less than shallow, warm. Activation volumes in all species were conserved at 30-60 ml mol-1 at physiological pressures, which may reflect a similar membrane physical state at the actual pressure the animal experiences. Arrhenius plots [In(Na+/K+-ATPase activity) vs 1/T] were steeper for warm-water and shallow-living species than for deep-sea species. The depth at which adaptation was first observed was about 2000 m (approximately equal to 200 atm: 1 atm = 101.3 kPa). The data are consistent with a model of increased membrane fluidity resulting in reduced pressure-sensitivity of Na+/K+-ATPase from deep-sea species.
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