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Merck
CN

C3260

Citrate Synthase from porcine heart

ammonium sulfate suspension, ≥100 units/mg protein

Synonym(s):

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

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About This Item

CAS Number:
9027-96-7
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
4.1.3.7 (BRENDA, IUBMB)
MDL number:
MFCD00130808

Key Documents

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Product Name

Citrate Synthase from porcine heart, ammonium sulfate suspension, ≥100 units/mg protein

biological source

Porcine heart

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

Quality Level

200

Other Notes

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.

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.

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

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

低风险生物材料
动植物源性产品
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Certificates of Analysis (COA)

Lot/Batch Number
SLCC7842
SLBW4809
SLBS4413
SLBM7486V
SLBJ0729V

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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
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
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
Hairui Yuan et al.
PloS one, 8(1), e53887-e53887 (2013-01-18)
Aerobic exercise has beneficial effects on both weight control and skeletal muscle insulin sensitivity through a number of specific signaling proteins. To investigate the targets by which exercise exerts its effects on insulin resistance, an approach of proteomic screen was
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
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