P7173
Pyruvate Carboxylase from bovine liver
buffered aqueous glycerol solution, 5-25 units/mg protein (BCA)
Synonyme(s) :
Pyruvate:CO2 ligase (ADP-forming)
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.26
MDL number:
Specific activity:
5-25 units/mg protein (BCA)
Concentration:
≥0.5 mg/mL
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buffered aqueous glycerol solution
Quality Level
specific activity
5-25 units/mg protein (BCA)
concentration
≥0.5 mg/mL
foreign activity
lactic dehydrogenase ≤0.5%
storage temp.
−20°C
Application
Pyruvate is critical for gluconeogenesis, lipogenesis, glyceroneogenesis, neurotransmitter biosynthesis and glucose-induced insulin, and is used to study these processes.
The enzyme from Sigma has been used as a positive control during the assay of pyruvate carboxylase activity in cell-free extracts of Corynebacterium glutamicum.
Biochem/physiol Actions
Pyruvate carboxylase catalyzes the carboxylation of pyruvate to oxaloacetate. Pyruvate carboxylase is a mitochondrial protein that has a biotin prosthetic group that requiries magnesium or manganese and acetyl CoA.
Physical form
Solution in 50% glycerol containing 0.05 M Tris-HCl, pH 7.4, 2 mM magnesium acetate and 1 mM EDTA.
Preparation Note
Affinity purified
Other Notes
One unit will convert 1.0 μmole of pyruvate and CO2 to oxalacetate per min at pH 7.8 at 30 °C.
Classe de stockage
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Contenu apparenté
QC Methods
H M White et al.
Journal of dairy science, 95(3), 1249-1256 (2012-03-01)
Expression of mRNA for pyruvate carboxylase (PC) is elevated at calving and during other physiological states when plasma NEFA concentrations are increased. The objective of this study was to determine the direct effects of fatty acids on expression of PC
Scott B Crown et al.
BMC systems biology, 6, 43-43 (2012-05-18)
¹³C-Metabolic flux analysis (¹³C-MFA) is a standard technique to probe cellular metabolism and elucidate in vivo metabolic fluxes. 13C-Tracer selection is an important step in conducting ¹³C-MFA, however, current methods are restricted to trial-and-error approaches, which commonly focus on an
Abdussalam Adina-Zada et al.
Biochemistry, 51(41), 8208-8217 (2012-09-19)
Mutation of Arg427 and Arg472 in Rhizobium etli pyruvate carboxylase to serine or lysine greatly increased the activation constant (K(a)) of acetyl CoA, with the increase being greater for the Arg472 mutants. These results indicate that while both these residues