Results 181 to 190 of about 2,702 (229)
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Pyruvate carboxylase: Affinity labelling of the pyruvate binding site

Biochemical and Biophysical Research Communications, 1975
Abstract The active-site-directed reagent, bromopyruvate has been used to covalently label the pyruvate binding site of pyruvate carboxylase (E.C.6.4.1.1.) isolated from sheep liver. Oxalo-acetate proved to be the most effective reaction component in protecting the enzyme against inactivation; pyruvate was less effective although its efficiency was ...
P J, Hudson, D B, Keech, J C, Wallace
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Effects of pyruvate on pyruvate dehydrogenase kinase of rat heart

Molecular and Cellular Biochemistry, 1995
Sensitivity of rat heart pyruvate dehydrogenase kinase (PDHK) to pyruvate inhibition was tested under various conditions using pyruvate dehydrogenase complex (PDC) in mitochondria (mPDC) and in a high speed precipitate of whole tissue homogenates (hPDC).
T C, Carter, H G, Coore
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Pyruvate kinase activators for treatment of pyruvate kinase deficiency

Hematology, 2023
Abstract Pyruvate kinase (PK) deficiency is a congenital hemolytic anemia with wide-ranging clinical symptoms and complications associated with significant morbidity and reduced health-related quality of life in both children and adults.
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Pyruvate inhibition of pyruvate dehydrogenase kinase is a physiological variable

Biochemical and Biophysical Research Communications, 1985
Pyruvate inhibited pyruvate dehydrogenase kinase activity in mitochondria from adipose tissue, heart, brain and kidney of fed rats. Starvation for 24 h led to increased kinase activity in mitochondria from adipose tissue and heart but not from brain or kidney and to reduction of pyruvate inhibition of the enzyme from adipose tissue, heart and brain ...
D, Lyn, H G, Coore
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Regulation of pyruvate carboxylase activity by pyruvate in mice liver

International Journal of Biochemistry, 1979
Abstract 1. 1. In order to study in vivo the possible regulatory role of pyruvate concentrations on pyruvate carboxylase activity. fed or 24 hr-fasted mice received various overloads of unlabeled pyruvate. 2. 2. The effect of these overloads on the incorporation of [2- 14 C]pyruvate into blood glucose was studied. 3. 3.
S, Bas, P, Favarger, S, Rous
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Assays of Pyruvate Dehydrogenase Complex and Pyruvate Carboxylase Activity

2011
Pyruvate dehydrogenase complex (PDC) and pyruvate carboxylase (PC) are mitochondrial enzymes that provide the initial steps of the two main alternatives for pyruvate metabolism: oxidative decarboxylation vs. anaplerotic carboxylation, gluconeogenesis, and glycerogenesis.
Douglas, Kerr   +2 more
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Bioelectrocatalysis of Pyruvate with PQQ-dependent Pyruvate Dehydrogenase

ECS Transactions, 2010
Although pyruvate has not been considered as a fuel for an enzymatic biofuel cell, there are dehydrogenase enzyme capable of oxidizing pyruvate. This paper details the discovery of a pyrroloquinoline quinone-dependent pyruvate dehydrogenase (PQQ-PDH) in Gluconobacter species.
Becky L. Treu   +2 more
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Pyruvate Carboxylase and Pyruvate Dehydrogenase Deficiency

2014
Pyruvate carboxylase and pyruvate dehydrogenase deficiency are the most common disorders in pyruvate metabolism and almost always affect the central nervous system. The severity and the clinical phenotypes vary, with a range from overwhelming neonatal lactic acidosis and early death to milder presentations.
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“Fluorokinase” and pyruvic kinase

Archives of Biochemistry and Biophysics, 1958
Abstract 1. 1. The enzyme catalyzing the CO2-dependent phosphorylation of fluoride by adenosine triphosphate to yield monofluorophosphate, an activity referred to as “fluorokinase,” has been isolated in crystalline form from rabbit muscle extracts. The crystalline enzyme has been found to possess considerable pyruvic kinase activity. 2. 2.
A, TIETZ, S, OCHOA
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Pyruvate kinase deficiency

Clinical Biochemistry, 1990
Pyruvate kinase (PK) deficiency was initially described by Valentine et al. in 1961. Since then, more than 300 cases have been described, including 65 in Japan. PK deficiency is the most common hereditary nonspherocytic hemolytic anemia among several red cell enzyme defects of the Embden-Meyerhof glycolytic pathway.
S, Miwa, H, Fujii
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