Abstract
The content of spinach-leaf cells was compartmented by differential centrifugation. Three fractions were obtained,i.e. chloroplasts, pellet of remaining organelles sedimenting at 97 000g and cytosol. Enzyme activities of L-tryptophan aminotransferase (TAT) as well as L-tryptophan dehydrogenase (TDH) were demonstrated in all cell fractions. The highest activities of both enzymes were found in the pellet of organelles followed by the enzyme activities in the chloroplasts. The cytosol had the lowest enzyme activities. Chloroplasts are characterized by a relatively higher TDH activity, organelles sedimenting at 97 000g were marked by a relatively higher TAT activity. In all fractions both pyridine nucleotide coenzymes catalyzed the TDH activity. Ca2+ in a concentration of 0.8 minol l−1 increased markedly the TDH activity in both directions of its activity.
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Abbreviations
- 2-(N-morpholino) ethanesulfonic acid:
-
MES
- Na2-ethylenediaminotetraacetate dihydrate:
-
Na2EDTA.2 H2O
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An erratum to this article is available at http://dx.doi.org/10.1007/BF02894724.
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Vacková, K., Mehta, A. & Kutáček, M. Tryptophan aminotransferase and tryptophan dehydrogenase activities in some cell compartments of spinach leaves: The effect of calcium ions on tryptophan dehydrogenase. Biol Plant 27, 154–158 (1985). https://doi.org/10.1007/BF02902153
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DOI: https://doi.org/10.1007/BF02902153