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D-Ribulose 1,5-Diphosphate Carboxylase from spinach

partially purified powder, 0.01-0.1 unit/mg solid

3-Phospho-D-glycerate carboxy-lyase(dimerizing), Rubisco
CAS Number:
Enzyme Commission number:
MDL number:

Quality Level

biological source



partially purified powder

specific activity

0.01-0.1 unit/mg solid

mol wt

557 kDa

storage temp.


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


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


5 units in poly bottle
1 unit in poly bottle

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.

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.

Storage Class Code

13 - Non Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

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Jenna L Losh et al.
The New phytologist, 198(1), 52-58 (2013-01-25)
Ribulose 1,5 bisphosphate carboxylase oxygenase (Rubisco) concentrations were quantified as a proportion of total protein in eight species of microalgae. This enzyme has been assumed to be a major fraction of total protein in phytoplankton, as has been demonstrated in
Benjamin D Rae et al.
Microbiology and molecular biology reviews : MMBR, 77(3), 357-379 (2013-09-06)
Cyanobacteria are the globally dominant photoautotrophic lineage. Their success is dependent on a set of adaptations collectively termed the CO2-concentrating mechanism (CCM). The purpose of the CCM is to support effective CO2 fixation by enhancing the chemical conditions in the
Shunsuke Adachi et al.
Journal of experimental botany, 64(4), 1061-1072 (2013-01-26)
Increases in rates of individual leaf photosynthesis (P(n)) are critical for future increases in yields of rice plants. Although many efforts have been made to improve rice P(n) with transgenic technology, the desired increases in P(n) have not yet been
F Grant Pearce
The Biochemical journal, 399(3), 525-534 (2006-07-11)
During catalysis, all Rubisco (D-ribulose-1,5-bisphosphate carboxylase/oxygenase) enzymes produce traces of several by-products. Some of these by-products are released slowly from the active site of Rubisco from higher plants, thus progressively inhibiting turnover. Prompted by observations that Form I Rubisco enzymes
Moritz Meyer et al.
Journal of experimental botany, 64(3), 769-786 (2013-01-25)
The importance of the eukaryotic algal CO(2)-concentrating mechanism (CCM) is considered in terms of global productivity as well as molecular phylogeny and diversity. The three major constituents comprising the CCM in the majority of eukaryotes are described. These include: (i)

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