Results 261 to 270 of about 25,295 (321)

Lactate-induced autophagy activation: unraveling the therapeutic impact of high-intensity interval training on insulin resistance in type 2 diabetic rats. [PDF]

open access: yesSci Rep
Pirani H   +7 more
europepmc   +1 more source

Immunoevaluation of GLUT-1 in oral squamous cell carcinoma. [PDF]

open access: yesJ Oral Maxillofac Pathol
Doss DM   +5 more
europepmc   +1 more source

Pyruvate kinase activators for treatment of pyruvate kinase deficiency [PDF]

open access: greenHematology, 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.
Rachael F. Grace
openaire   +3 more sources

Dioxiranes Generated in Situ from Pyruvates and Oxone as Environmentally Friendly Oxidizing Agents for Disinfection [PDF]

open access: yesEnvironmental Science & Technology, 2006
Dioxiranes generated in situ from pyruvates (α-keto esters) and Oxone have been found to be environmentally friendly oxidizing agents for disinfection.
Man-Kin Wong
exaly   +3 more sources
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Pyruvate carboxylase

The International Journal of Biochemistry & Cell Biology, 1998
Pyruvate carboxylase [EC 6.4.1.1] is a member of the family of biotin-dependent carboxylases and is found widely among eukaryotic tissues and in many prokaryotic species. It catalyses the ATP-dependent carboxylation of pyruvate to form oxaloacetate which may be utilised in the synthesis of glucose, fat, some amino acids or their derivatives and several
Wallace, J.   +2 more
openaire   +3 more sources

Pyruvate carboxylase deficiency

Journal of Inherited Metabolic Disease, 1984
AbstractThe causes of congenital lactic acidaemia are outlined. Isolated pyruvate carboxylase deficiency is reviewed in detail with a report of a recent case and a discussion of the biochemical consequences. Other causes of defective pyruvate carboxylation are described, particularly the combined carboxylase defects.
K, Bartlett   +4 more
openaire   +2 more sources

Substrate activation of pyruvate carboxylase by pyruvate

Biochemical and Biophysical Research Communications, 1969
Abstract A kinetic analysis of pyruvate carboxylase isolated from sheep liver and using pyruvate as the variable substrate revealed non-Michaelis Menten kinetic. Double reciprocal plots were biphasic and R S values of 222 were obtained. Hill plots prepared from the initial velocity data showed that at low pyruvate concentrations, the slope of the ...
H, Taylor, J, Nielsen, D B, Keech
openaire   +2 more sources

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