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Volumn 213, Issue 3, 2001, Pages 379-389
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Partial purification and biochemical characterization of a heteromeric protein phosphatase 2A holoenzyme from maize (Zea mays L.) leaves that dephosphorylates C4 phosphoenolpyruvate carboxylase
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Author keywords
C4 phosphoenolpyruvate carboxylase; Enzyme purification (PP2A); PP2A holoenzyme; Serine threonine phosphatase; Zea (PP2A)
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Indexed keywords
AMINO ACID;
CHEMICAL ANALYSIS;
CYANOGINOSIN LR;
ENZYME INHIBITION;
ENZYME SPECIFICITY;
HOLOENZYME;
PHOSPHOENOLPYRUVATE CARBOXYLASE;
PHOSPHOPROTEIN PHOSPHATASE 2A;
PHOTOSYNTHESIS;
PLANT LEAF;
PROTEIN PURIFICATION;
PROTEIN SUBUNIT;
SENSITIVITY;
SERINE;
BIOCHEMISTRY;
CHROMATOGRAPHIC ANALYSIS;
ENZYME INHIBITION;
IMMUNOLOGY;
LIGHTING;
METABOLITES;
PHOSPHATES;
PHOTOSYNTHESIS;
PURIFICATION;
SUBSTRATES;
PUTATIVE;
PLANTS (BOTANY);
DARKNESS;
HOLOENZYMES;
ISOTOPE LABELING;
LIGHT;
MOLECULAR WEIGHT;
PHOSPHOENOLPYRUVATE CARBOXYLASE;
PHOSPHOPROTEIN PHOSPHATASE;
PHOSPHORYLATION;
PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS;
PLANT LEAVES;
PROTEIN PROCESSING, POST-TRANSLATIONAL;
PROTEIN-SERINE-THREONINE KINASES;
ZEA MAYS;
EUKARYOTA;
MAMMALIA;
ORYCTOLAGUS CUNICULUS;
ZEA;
ZEA MAYS;
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EID: 0034928181
PISSN: 00320935
EISSN: None
Source Type: Journal
DOI: 10.1007/s004250100604 Document Type: Article |
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Times cited : (29)
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References (39)
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