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Intracellular location of NADP+-linked malic enzyme in C3plants

✍ Scribed by Hamed M. El-Shora; Tom Rees

Publisher
Springer-Verlag
Year
1991
Tongue
English
Weight
645 KB
Volume
185
Category
Article
ISSN
0032-0935

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✦ Synopsis

The aim of this work was to determine the maximum catalytic activity and intracellular location of NADP+-linked malic enzyme (EC 1.1.1.40) in C3 plants. Appreciable activities, ranging from 80 to 712 nmol 9 (gFW)-1 . min-1, were found in a wide range of tissues (roots and leaves of Pisum sativum L., cotyledons of Cucurbita pepo Alef., developing seeds of Brassica napus L., mesocarp of Persea americana Gaertn., and suspension cultures of Glycine max L.). Overall, activity showed a rough positive correlation with biosynthesis. Differential and density-gradient fractionation of extracts of the cotyledons of germinating marrow (C. pepo) and lysates of protoplasts of suspension cultures of G. showed that the enzyme had the same distribution as the plastid marker enzymes. It is suggested that in C3 plants NADP+-linked malic enzyme is confined to the plastids and involved in biosynthesis.

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Two forms of NADP-dependent malic enzyme
Two forms of NADP-dependent malic enzyme in expanding maize leaves
✍ Paolo Pupillo; Patrizia Bossi πŸ“‚ Article πŸ“… 1979 πŸ› Springer-Verlag 🌐 English βš– 622 KB

Etiolated maize leaves (Zea mays L.) contain a major isozyme of NADP-dependent malic enzyme (L-malate dehydrogenase, decarboxylating, EC 1.1.1.40) having an isoelectric point of 5.28Β±0.03, a Km (L-malate) 0.3-0.6 mM at pH 7.45; a broad pH optimum around pH 6.9 under the conditions of assay; a molecu