Purification and properties of a chloroplastic phosphatase distinct from fructose bisphosphatase
- 1 September 1984
- journal article
- research article
- Published by Elsevier in Plant Science Letters
- Vol. 36 (2), 137-142
- https://doi.org/10.1016/0304-4211(84)90248-7
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Affinity chromatography, on fructose‐bisphosphatase–Sepharose, of two chloroplastic thioredoxins FEuropean Journal of Biochemistry, 1984
- Activation of wheat chloroplast sedoheptulose bisphosphatase: A continuous spectrophotometric assayArchives of Biochemistry and Biophysics, 1982
- Molecular Properties of Chloroplastic Thioredoxin f and the Photoregulation of the Activity of Fructose 1,6-BisphosphataseEuropean Journal of Biochemistry, 1981
- A rapid method for isolation of purified, physiologically active chloroplasts, used to study the intracellular distribution of amino acids in pea leavesPlanta, 1980
- Chloroplast Sedoheptulose 1,7-Bisphosphatase: Evidence for Regulation by the Ferredoxin/Thioredoxin SystemZeitschrift für Naturforschung C, 1978
- Efficient Purification and Molecular Properties of Spinach Chloroplast Fructose 1,6‐BisphosphataseEuropean Journal of Biochemistry, 1976
- Appearance of sedoheptulose 1,7-diphosphatase activity on conversion of chloroplast fructose 1,6-diphosphatase from dimer form to monomer formBiochemical and Biophysical Research Communications, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Determination of Molecular Weights of Proteins by Gel Filtration of Sephadex.Analytical Chemistry, 1963