Effect of ligand binding and of pH change on the accessibility of thiol residues of fructose-1,6-bisphosphatase from spinach chloroplast
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference17 articles.
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Cited by 10 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Activation properties of the redox-modulated chloroplast enzymes glyceraldehyde 3-phosphate dehydrogenase and fructose-1,6-bisphosphatase;Physiologia Plantarum;2008-07-18
2. Activation properties of the redox-modulated chloroplast enzymes glyceraldehyde 3-phosphate dehydrogenase and fructose-1,6-bisphosphatase;Physiologia Plantarum;2000-11
3. Plant fructose-1,6-bisphosphatases: characteristics and properties;International Journal of Biochemistry;1992-08
4. Enzymes of the Calvin Cycle;Methods in Plant Biochemistry;1990
5. Concerted action of cosolvents, chaotropic anions and thioredoxin on chloroplast fructose-1,6-bisphosphatase. Reactivity to iodoacetamide;European Journal of Biochemistry;1989-11
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