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R8000

Sigma-Aldrich

D-Ribulose 1,5-Diphosphate Carboxylase from spinach

partially purified powder, 0.01-0.1 unit/mg solid

Synonym(s):

3-Phospho-D-glycerate carboxy-lyase(dimerizing), Rubisco

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1 UNIT
$193.80
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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

$193.80

List price$204.00
Web-Only Promotion

Available to ship onApril 08, 2025Details


biological source

spinach

form

partially purified powder

specific activity

0.01-0.1 unit/mg solid

mol wt

557 kDa

storage temp.

−20°C

Related Categories

General description

D-Ribulose 1,5-Diphosphate Carboxylase (RUBISCO) amounts to 50% of the total spinach leaves associated soluble protein.[1]
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[2]
  • as an innocuous or non-hazardous protein sample to test its effect on human intestinal epithelial cell lines[3]
  • in isothermal titration calorimetry (ITC), and radiolabeled binding assays with abscisic acid[4]

Biochem/physiol Actions

D-Ribulose 1,5-Diphosphate Carboxylase (RUBISCO) depends on Rubisco activase and chaperones for activation.[5] It participates in plant photorespiration events by catalyzing the carboxylation and oxygenation of ribulose-1,5-bisphosphate.[1] Abscisic acid inhibits the carboxylation activity of Rubisco.[4]

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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K Thomas et al.
Regulatory toxicology and pharmacology : RTP, 39(2), 87-98 (2004-03-26)
Rationale. Evaluation of the potential allergenicity of proteins derived from genetically modified foods has involved a weight of evidence approach that incorporates an evaluation of protein digestibility in pepsin. Currently, there is no standardized protocol to assess the digestibility of
Martin A J Parry et al.
Journal of experimental botany, 64(3), 717-730 (2012-11-20)
Rubisco (ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase) enables net carbon fixation through the carboxylation of RuBP. However, some characteristics of Rubisco make it surprisingly inefficient and compromise photosynthetic productivity. For example, Rubisco catalyses a wasteful reaction with oxygen that leads to the release
Guillaume Tcherkez
Plant, cell & environment, 36(9), 1586-1596 (2013-01-12)
Although ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) was discovered nearly 60 years ago, the associated chemical mechanism of the reaction is still incompletely understood. The catalytic cycle consists of four major steps: ribulose-1,5-bisphosphate binding, enolization, CO₂ or O₂ addition and hydration, and cleavage
Inger Andersson
Journal of experimental botany, 59(7), 1555-1568 (2008-04-18)
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the incorporation of inorganic CO(2) into the organic molecules of life. Rubisco is extremely inefficient as a catalyst and its carboxylase activity is compromised by numerous side-reactions including oxygenation of its sugar phosphate substrate by atmospheric
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

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