Science · 1979 · 19 citations · 20 references
Life SciencesBiochemistryMolecular BiologyEnzymologyPlant BiochemistryProtein BiochemistryEnzyme CharacterizationEnzyme KineticsPlant EnzymesProtein AnalysisProtein ChemistryCrystalline StructureGel ElectrophoresisMolecular Weight DeterminationProtein Separation TechniquesRubisco ActivitySodium Dodecyl Sulfate-polyacrylamide Gel ElectrophoresisVapor Diffusion
Spinach fraction I protein (ribulose 1,5-bisphosphate carboxylase-oxy genase, E.C. 4.1.1.39) was crystallized on both an analytical and a preparative scale by vapor diffusion with polyethylene glycol (molecular weight, 6000) used as the precipitant. The identity of the crystalline material with fraction I protein was shown by gel electrophoresis in the presence of sodium dodecyl sulfate and immunological properties. The carboxylase and oxygenase activities copurify during crystallization, and the crystalline enzyme lacks copper and iron.
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d-Ribulose-1,5-bisphosphate carboxylase-oxygenase
George H. Lorimer, Murray R. Badger, T. John Andrews · Analytical Biochemistry · 1977 · 335 citations
Nobumaro Kawashima, S. G. Wildman · Annual Review of Plant Physiology · 1970 · 293 citations