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C3260

Sigma-Aldrich

Citrate Synthase from porcine heart

ammonium sulfate suspension, ≥100 units/mg protein

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Synonym(s):
Citrate condensing enzyme, Citrate oxaloacetate lyase (CoA-acetylating)
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

biological source

Porcine heart

Quality Level

form

ammonium sulfate suspension

specific activity

≥100 units/mg protein

mol wt

98 kDa ( 49 kDa monomer)

solubility

H2O: soluble 1.0 mg/mL, clear

foreign activity

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

storage temp.

2-8°C

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This Item
G9880L7525E2884
vibrant-m

C3260

Citrate Synthase from porcine heart

vibrant-m

E2884

Esterase from porcine liver

specific activity

≥100 units/mg protein

specific activity

≥75 units/mg protein

specific activity

≥200 units/mg protein

specific activity

≥150 units/mg protein (biuret)

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

ammonium sulfate suspension

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

solubility

H2O: soluble 1.0 mg/mL, clear

solubility

-

solubility

-

solubility

-

mol wt

98 kDa ( 49 kDa monomer)

mol wt

42 kDa

mol wt

-

mol wt

168 kDa

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

Biochem/physiol Actions

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.

Unit Definition

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

Physical form

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

Preparation Note

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

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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
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
Adam Begeman et al.
EMBO reports, 21(10), e49735-e49735 (2020-09-19)
Maintaining proteome health is important for cell survival. Nucleic acids possess the ability to prevent protein aggregation more efficiently than traditional chaperone proteins. In this study, we explore the sequence specificity of the chaperone activity of nucleic acids. Evaluating over
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)

Articles

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