The dark (oxidized) form of the light-activatable NADP-malate dehydrogenase from pea chloroplasts is catalytically active in the presence of guanidine-HCl-Reference-Cited by-同舟云学术

The dark (oxidized) form of the light-activatable NADP-malate dehydrogenase from pea chloroplasts is catalytically active in the presence of guanidine-HCl

Published:1985-01-28 Issue:2 Volume:180 Page:317-320
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Scheibe R.,Fickenscher K.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(85)81094-2/fullpdf

Reference13 articles.

1. Properties and regulation of leaf nicotinamide–adenine dinucleotide phosphate–malate dehydrogenase and ‘malic’ enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis

2. Light Modulation of Enzyme Activity in Chloroplasts

3. Dithiothreitol: An inhibitor of glucose-6-phosphate-dehydrogenase activity in leaf extracts and isolated chloroplasts

4. Regulation of NADP-malate dehydrogenase by the light-actuated ferredoxin/thioredoxin system of chloroplasts

5. Quantitation of the thiol groups involved in the reductive activation of NADP: Malate dehydrogenase

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1. Flux Control of the Malate Valve in Leaf Cells;Archives of Biochemistry and Biophysics;1998-01

2. Starch degradation in chloroplasts isolated from C3 or CAM (crassulacean acid metabolism)-induced Mesembryanthemum crystallinum L;Biochemical Journal;1996-09-15

3. Malate dehydrogenase (NADP+);Enzyme Handbook 9;1995

4. Cysteines of chloroplast NADP-malate dehydrogenase form mixed disulfides;FEBS Letters;1994-12-05

5. Cloning, site-specific mutagenesis, expression and characterization of full-length chloroplast NADP-malate dehydrogenase from Pisum sativum;European Journal of Biochemistry;1993-10