Results 101 to 110 of about 191,179 (159)
Journal of Biological Chemistry, 1965 Some of the next articles are maybe not open access.
Related searches:
Related searches:
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 [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, 1984AbstractThe 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, 1969Abstract 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
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
openaire +2 more sources
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
openaire +2 more sources
Current Opinion in Anaesthesiology, 2008
Ethyl pyruvate is a simple derivative of the endogenous metabolite, pyruvic acid. Ethyl pyruvate was shown to ameliorate some of the structural and functional changes associated with mesenteric ischemia and reperfusion in rats.Treatment with ethyl pyruvate has been shown to improve survival and ameliorate organ dysfunction in a wide variety of ...
openaire +2 more sources
Ethyl pyruvate is a simple derivative of the endogenous metabolite, pyruvic acid. Ethyl pyruvate was shown to ameliorate some of the structural and functional changes associated with mesenteric ischemia and reperfusion in rats.Treatment with ethyl pyruvate has been shown to improve survival and ameliorate organ dysfunction in a wide variety of ...
openaire +2 more sources
Transpulmonary pyruvate kinetics
American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 2011Shuttling of intermediary metabolites, such as pyruvate, contributes to the dynamic energy and biosynthetic needs of tissues. Tracer kinetic studies offer a powerful tool to measure the metabolism of substrates like pyruvate that are simultaneously taken up from and released into the circulation by organs.
Matthew L, Johnson +3 more
openaire +2 more sources
Amperometric sensor for pyruvate with immobilized pyruvate oxidase
Analytica Chimica Acta, 1987Abstract Several procedures for immobilization of pyruvate oxidase by chemical bonding are reported. Attachment to nylon net was unsatisfactory in terms of yield and stability. Polyazetidine, a new commercially available prepolymer and a new nylon membrane with surface carboxyl groups provided good long-term stability, up to 30 days in the case of ...
M. Mascini, MAZZEI, Franco
openaire +1 more source
Pyruvate carboxylase: Affinity labelling of the pyruvate binding site
Biochemical and Biophysical Research Communications, 1975Abstract 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
openaire +2 more sources