Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

D-Ribulose 1,5-Diphosphate Carboxylase from spinach has been used: as a test protein in pepsin digestion studiesas an innocuous or non-hazardous protein sample to test its effect on human intestinal epithelial cell linesin 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.

General description

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. K_M 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.

D-Ribulose 1,5-Diphosphate Carboxylase (RUBISCO) amounts to 50% of the total spinach leaves associated soluble protein.

Packaging

1 unit in poly bottle

5 units in poly bottle

Unit Definition

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.