Ugrás a tartalomra
Merck

R8000

Sigma-Aldrich

D-Ribulose 1,5-Diphosphate Carboxylase from spinach

partially purified powder, 0.01-0.1 unit/mg solid

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
MDL-szám:
UNSPSC kód:
12352204
NACRES:
NA.54

biológiai forrás

spinach

Minőségi szint

Forma

partially purified powder

specifikus aktivitás

0.01-0.1 unit/mg solid

molekulatömeg

557 kDa

tárolási hőmérséklet

−20°C

Általános leírás

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.

Alkalmazás

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

Biokémiai/fiziológiai hatások

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.

Egység definíció

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.

Piktogramok

Health hazard

Figyelmeztetés

Danger

Figyelmeztető mondatok

Óvintézkedésre vonatkozó mondatok

Veszélyességi osztályok

Resp. Sens. 1

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, type N95 (US)


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Dennis McNevin et al.
Journal of experimental botany, 57(14), 3883-3900 (2006-10-19)
The forward and reverse rate constants involved in carbamylation, activation, carboxylation, and inhibition of D-ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) have been estimated by a new technique of simultaneous non-linear regression of a differential equation kinetic model to multiple experimental data. Parameters predicted
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
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
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
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

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