Alkaline inorganic pyrophosphatase and starch synthesis in amyloplasts |
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Authors: | P Gross T ap Rees |
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Institution: | (1) Botany School, University of Cambridge, Downing Street, CB2 3EA Cambridge, UK;(2) Present address: Institut für Biochemie der Pflanze, Universität Göttingen, Untere Karspüle 2, D-3400 Göttingen, Germany |
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Abstract: | The aim of this work was to see if amyloplasts contained inorganic pyrophosphatase. Alkaline pyrophosphatase activity, largely dependant upon MgCl2 but not affected by 100 M ammonium molybdate or 60–100 mM KCl, was demonstrated in exracts of developing and mature clubs of the spadix of Arum maculatum L. and of suspension cultures of Glycine max L., but not in extracts of the developing bulb of Allium cepa L. The maximum catalytic activity of alkaline pyrophosphatase in the above tissues showed a positive correlation with starch synthesis, and in the first two tissues was shown to exceed the activity of ADPglucose pyrophosphorylase. Of the alkaline pyrophosphatase activity in lysates of protoplasts of suspension cultures of Glycine max, 57% was latent. Density-gradient centrifugation of these lysates showed a close correlation between the distribution of alkaline pyrophosphatase and the plastid marker, nitrite reductase. It is suggested that much, if not all, of the alkaline pyrophosphatase in suspension cultures of Glycine max is located in the plastids.Abbreviations PPase
inorganic pyrophosphatase
- PPi
inorganic pyrophosphate |
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Keywords: | Alkaline pyrophosphatase Amyloplast Arum (starch synthesis) Glycine (starch synthesis) Starch synthesis |
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