Mitochondrial ATPase in the gills of the shore crabCarcinus maenas |
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Authors: | D Siebers J Hentschel K Böttcher C Lucu |
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Institution: | 1. Biologische Anstalt Helgoland, Notkestr. 31, D-W-2000, Hamburg 52, Federal Republic of Germany 2. Fakult?t für Biologie, Universit?t Konstanz, Universit?tsstr. 10, D-W-7750, Konstanz 1, Federal Republic of Germany 3. Center for Marine Research, Ruder Boskovic Institute, 52210, Bovinj, Croatia
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Abstract: | Posterior gills (No. 7 and 8) of shore crabsCarcinus maenas were homogenized and fractionated by means of differential and density gradient centrifugation. Employment of marker enzymes
Na-K-ATPase and carbonic anhydrase for plasma membranes and cytochrome oxidase for mitochondria showed that these structural
elements were separated. Ultramicroscopic investigations of combined fractions confirmed the presence of the respective mitochondrial
and vesicular plasma membrane structures. An ATPase which did not depend on the presence of sodium (20 mM) ions in the incubation
medium but on the presence of potassium (20 mM) ions only was found in the mitochondrial fractions. The mitochondrial ATPase
was tightly bound to cellular particulates and activated approximately threefold by bicarbonate (20 mM) ions. The activity
of this ATPase was nearly completely inhibited by oligomycin (1 μg ml−1) and greatly inhibited by low levels (5 mM) of thiocyanate and calcium ions, the Ki for Ca2+ being ca 4 mM. The results obtained confirm literature data on high mitochondrial densities in crab gills and allow the assumption
of significant rates of energy metabolism in these organs. Considering its properties the mitochondrial ATPase is clearly
distinct from crab gill Na-K-ATPase and can be measured specifically in samples containing Na-K-ATPase. Mitochondrial ATPase
is therefore considered a suitable and reliable marker enzyme for mitochondria. |
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