Merck, R8000-5UN, D-Ribulose 1,5-Diphosphate Carboxylase from spinach

General description
D-Ribulose 1,5-Diphosphate Carboxylase (RUBISCO) amounts to 50% of the total spinach leaves associated soluble protein.
Exists as a 557 kDa hexadecamer composed of eight heavy chains each with a molecular weight of approximately 56 kDa and eight light chains of molecular weight 14 kDa. Each molecule contains one magnesium ion.
pH optimum: ~7.9.
KM for CO2: ~0.45 mM.
Ribulose diphosphate becomes inhibitory at concentrations exceeding 0.7 mM. Orthophosphate and ammonium sulfate are competitive inhibitors. 3-Phosphoglycerate is a noncompetitive inhibitor.
Application
D-Ribulose 1,5-Diphosphate Carboxylase from spinach has been used:
as a test protein in pepsin digestion studies
as an innocuous or non-hazardous protein sample to test its effect on human intestinal epithelial cell lines
in isothermal titration calorimetry (ITC), and radiolabeled binding assays with abscisic acid

Biochem/physiol Actions
D-Ribulose 1,5-Diphosphate Carboxylase (RUBISCO) depends on Rubisco activase and chaperones for activation. It participates in plant photorespiration events by catalyzing the carboxylation and oxygenation of ribulose-1,5-bisphosphate. Abscisic acid inhibits the carboxylation activity of Rubisco.
Other Notes
One unit will convert 1.0 μmole of D-RuDP and CO2 to 2.0 μmoles of D-3-phosphoglycerate per min at pH 7.8 at 25°C.