Ferredoxin-NADP+ oxidoreductase is active as a monomer with molecular weight 33,000–36,000
- 1 December 1980
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 205 (2), 499-502
- https://doi.org/10.1016/0003-9861(80)90132-0
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Studies of the multiple forms of ferredoxin-NADP oxidoreductase from spinachArchives of Biochemistry and Biophysics, 1979
- Studies on the Ferredoxin–Ferredoxin-NADP Reductase Complex: Kinetic and Solvent Perturbation Studies on the Location of Sulfhydryl and Aromatic Amino Acid ResiduesThe Journal of Biochemistry, 1978
- Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leavesBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Multiple forms of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase from spinachArchives of Biochemistry and Biophysics, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Combined preparation of ferredoxin, ferredoxin-NADP+ reductase and plastocyanin from spinach leavesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1970
- On the Structure and Function of Reduced Nicotinamide Adenine Dinucleotide Phosphate‐Cytochrome f Reductase of Spinach ChloroplastsEuropean Journal of Biochemistry, 1968
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- Ultraviolet absorption spectra of DPN and analogs of DPNArchives of Biochemistry and Biophysics, 1959
- Apparent Specific Volume of α-Casein and β-Casein and the Relationship of Specific Volume to Amino Acid CompositionJournal of the American Chemical Society, 1949