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Merck

C3260

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:
UNSPSC Code:
12352204
NACRES:
NA.54
Numéro CE :
MDL number:

Nom du produit

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

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.

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.

Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Consulter la Bibliothèque de documents

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
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
The Ca2+ increase by the sperm factor in physiologically polyspermic newt fertilization: its signaling mechanism in egg cytoplasm and the species-specificity
Harada Y, et al.
Developmental Biology, 351(2), 266-276 (2011)
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

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