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C3260

Sigma-Aldrich

Citrate Synthase from porcine heart

ammonium sulfate suspension, ≥100 units/mg protein

Synonyme(s) :

Citrate condensing enzyme, Citrate oxaloacetate lyase (CoA-acetylating)

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About This Item

Numéro CAS:
9027-96-7
Numéro de classification (Commission des enzymes):
4.1.3.7 (BRENDA, IUBMB)
Numéro MDL:
MFCD00130808
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

Porcine heart

Niveau de qualité

200

Forme

ammonium sulfate suspension

Activité spécifique

≥100 units/mg protein

Poids mol.

98 kDa ( 49 kDa monomer)

Solubilité

H2O: soluble 1.0 mg/mL, clear

Activité étrangère

isocitrate dehydrogenase and aconitase ≤0.01%
malic dehydrogenase ≤0.1%

Température de stockage

2-8°C

Application

Citrate Synthase from porcine heart has been used:
  • to inject newt egg for determining its importance in egg activation at fertilization
  • in the preparation of reaction mix to determine pyruvate carboxylase enzyme activity
  • to examine whether it can induce a [Ca2+] increase and egg activation in unfertilized eggs

Actions biochimiques/physiologiques

Citrate synthase catalyses the conversion of citrate to acetyl-CoA in the presence of coenzyme-A with the release of H2O and oxaloacetate. The enzyme has a molecular weight of 85 kDa and a pI of 6.1-6.6. It is inhibited by fluoroacetyl-CoA, palmitoyl-CoA, and citroyl-CoA. It is also inhibited when it is acetylated by acetic anhydride or iodinated by iodine.

Définition de l'unité

One unit will form 1.0 μmole of citrate from oxalacetate and acetyl CoA per min at pH 8.0 at 37 °C.

Forme physique

Suspension in 3.2 M (NH4)2SO4 solution, pH 7.0.

Notes préparatoires

Dissolves in water to form a clear solution at 1 mg/mL concentration.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Florian Stengel et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(5), 2007-2012 (2010-02-06)
Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that prevent protein aggregation by binding clients destabilized during cellular stress. Here we probe the architecture and dynamics of complexes formed between an oligomeric sHSP and client by
Oded Rimon et al.
Antioxidants & redox signaling, 27(15), 1252-1267 (2017-04-11)
A recently discovered group of conditionally disordered chaperones share a very unique feature; they need to lose structure to become active as chaperones. This activation mechanism makes these chaperones particularly suited to respond to protein-unfolding stress conditions, such as oxidative
Xiangjian Gou et al.
Plant biotechnology journal, 20(7), 1417-1431 (2022-04-11)
Single amino acid substitution (SAAS) produces the most common variant of protein function change under physiological conditions. As the number of SAAS events in plants has increased exponentially, an effective prediction tool is required to help identify and distinguish functional
Skylar Xantus Kim et al.
eLife, 7 (2018-07-17)
Anhydrobiotes are rare microbes, plants and animals that tolerate severe water loss. Understanding the molecular basis for their desiccation tolerance may provide novel insights into stress biology and critical tools for engineering drought-tolerant crops. Using the anhydrobiote, budding yeast, we
Alterations in Cytosolic and Mitochondrial [U-13C] Glucose Metabolism in a Chronic Epilepsy Mouse Model
McDonald TS, et al.
eNeuro, 4(1), 266-276 (2017)
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