Results 251 to 260 of about 128,438 (311)
Discovery of Cell-Permeable Allosteric Inhibitors of Liver Pyruvate Kinase: Design and Synthesis of Sulfone-Based Urolithins. [PDF]
Iqbal S+11 more
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Age-Related Changes in the Glycolytic Enzymes of M2-Isoform of Pyruvate Kinase and Fructose-1,6-Bisphosphate Aldolase: Implications to Age-Related Macular Degeneration. [PDF]
Rajala A, Rajala RVS.
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Regulation of Ptbp1-controlled alternative splicing of pyruvate kinase muscle by liver kinase B1 governs vascular smooth muscle cell plasticity in vivo. [PDF]
Cai Z+9 more
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Human Mutation, 1996
Pyruvate kinase (PK) deficiency due to mutations of the PKLR gene is a common cause of hereditary nonspherocytic hemolytic anemia. Thus far, 55 different mutations have been described in patients with PK-deficient hemolytic anemia. Polymorphisms within the PKLR gene and in the tightly linked glucocerebrosidase (GBA) gene suggest that PK deficiency may ...
Ernest Beutler, Luciano Baronciani
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Pyruvate kinase (PK) deficiency due to mutations of the PKLR gene is a common cause of hereditary nonspherocytic hemolytic anemia. Thus far, 55 different mutations have been described in patients with PK-deficient hemolytic anemia. Polymorphisms within the PKLR gene and in the tightly linked glucocerebrosidase (GBA) gene suggest that PK deficiency may ...
Ernest Beutler, Luciano Baronciani
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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.
Hisaichi Fujii, Shiro Miwa
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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.
Hisaichi Fujii, Shiro Miwa
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“Fluorokinase” and pyruvic kinase
Archives of Biochemistry and Biophysics, 1958Abstract 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.
Alisa Tietz, Severo Ochoa
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The stereochemistry of pyruvate kinase
Biochemical and Biophysical Research Communications, 1970Abstract α-Ketobutyrate enol phosphate consisting of approximately 80% cis and 20% trans isomers was prepared by the Perkow reaction. It was converted by pyruvate kinase in 2H2O, to α-ketobutyrate which on oxidative decarboxylation with hydrogen peroxide gave largely (2 R )-2- 2 H-propionate containing one atom of deuterium ...
David B. Sprinson, W.E. Bondinell
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Pyruvate kinase electrophoresis in normal and pyruvate kinase deficient hemolysates
Clinica Chimica Acta, 1974Abstract Two bands of pyruvate kinase activity were demonstrated in normal hemolysates with high voltage electrophoresis at pH 5.3 using cellulose acetate strips. Heterozygotes with red cell pyruvate kinase deficiency also exhibited two bands. Six of ten homozygous patients showed two bands, the remaining four only one band.
Bärbel Wonneberger, Werner Schröter
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