Pyruvate Dehydrogenase Complex (PDC)
Source: Bovine heart
Purity: > 90% by SDS-PAGE, subunit apparent Mr’s ~ 74,000 (E2), 53,000 (E3), 41,000 (E1a), 48,000 (E3-BP) and 36,000 (E1β). Apparent Mr ~ 8,500,000 by sedimentation equilibrium centrifugation.
Supplied: In 50 μl 50 mM Tris-HCl pH 7.0 buffer containing 14 mM β-mercaptoethanol, 1 mM benzamidine, 0.1 mM phenylmethanesulfonyl fluoride, 1 mM EDTA and 10% glycerol. Maintain in aliquots at -70° C. Avoid repeated thawing.
Activity: ~ 12-18 μmol of NADH formed per min per mg of protein with pyruvate as substrate
Background: The pyruvate dehydrogenase complex (PDC) is a mitochondrial enzyme which catalyzes the oxidative decarboxylation of pyruvate. PDC is regulated by reversible phosphorylation in response to extracellular stimuli. A tightly associated protein kinase phosphorylates and inactivates PDC. In contrast, loosely associated mitochondiral protein phosphatases dephosphorylate and activate PDC.
References: Methods Enzymol 166: 321 Methods Enzymol 89:376
