Essentiality of the small subunit (B) in the catalysis of RuBP carboxylase/oxygenase is not related to substrate-binding in the large subunit (A)
- 1 July 1984
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 122 (2) , 763-769
- https://doi.org/10.1016/s0006-291x(84)80099-6
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Interaction of constituent subunits in ribulose 1,5-bisphosphate carboxylase from Aphanothece halophyticaArchives of Biochemistry and Biophysics, 1984
- Ribulose 1,5-bisphosphate carboxylase from the halophilic cyanobacterium Aphanothece halophyticaArchives of Biochemistry and Biophysics, 1983
- RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE-OXYGENASEAnnual Review of Biochemistry, 1983
- Protein liganding to the activator cation of ribulose bisphosphate carboxylaseBiochemistry, 1982
- Carbamate formation on the .epsilon.-amino group of a lysyl residue as the basis for the activation of ribulosebisphosphate carboxylase by carbon dioxide and magnesium(2+)Biochemistry, 1980
- Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogsBiochemistry, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976