In vitro and in vivo regulation of chJoroplast glyceraldehyde-3-phosphate dehydrogenase isozymes from Chenopodium rubrum. III. The molecular basis of the aggregation phenomenon: chloroplast glyceraldehyde-3-phosphate dehydrogenase as an ambiquitous enzyme
Author:
Publisher
Wiley
Subject
Cell Biology,Plant Science,Genetics,General Medicine,Physiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3054.1983.tb00906.x/fullpdf
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4. Association of Glyceraldehyde-3-Phosphate Dehydrogenase with the Particulate Fraction of Chicken Skeletal Muscle
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1. C-terminal truncation of spinach chloroplast NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase prevents inactivation and reaggregation;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1996-09
2. Circadian Rhythms, Membranes and Susceptibility to Environmental Factors;Membranes and Circadian Rythms;1996
3. Properties to two high-molecular-mass forms of glyceraldehyde-3-phosphate dehydrogenase from spinach leaf, one of which also possesses latent phosphoribulokinase activity;European Journal of Biochemistry;1991-12
4. The physiological significance of aggregation phenomena of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1985-11
5. Enzyme patterns in energy metabolism during flower induction in spinach leaves;Plant, Cell and Environment;1985-07
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