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Cloning and characterization of a cDNA for the cytosolic isozyme of plant pyruvate kinase: the relationship between the plant and non-plant enzyme

โœ Scribed by Stephen D. Blakeley; William C. Plaxton; David T. Dennis

Publisher
Springer
Year
1990
Tongue
English
Weight
388 KB
Volume
15
Category
Article
ISSN
0167-4412

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โœฆ Synopsis

Pyruvate kinase (ATP: pyruvate phosphotransferase, EC 2.7.1.40) is a key glycolytic enzyme that catalyzes the formation of pyruvate and ATP from phoshoenolpyruvate and ADP. The enzyme from several non-plant sources has been purified and studied extensively [8,9,12,15,18]. Most of these enzymes are homotetrameric with a native Mr of 190-250 kDa. In plants, pyruvate kinase

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โœ Nishith Shah; J. William Bradbeer ๐Ÿ“‚ Article ๐Ÿ“… 1994 ๐Ÿ› Springer-Verlag ๐ŸŒ English โš– 540 KB

The chloroplastic and cytosolic isoenzymes of phosphoglycerate kinase (PGK; EC 2.7.2.3) of leaves from 18 of a broad range of 21 vascular plant species were separated by either standard or modified anion-exchange chromatographic procedures. Immunoprecipitation of the isoenzymes with antisera raised