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Nihon rinsho. Japanese journal of clinical medicine, 1973
PK deficiency is the most common and well characterized erythroenzymopathy in the Embden-Meyerhof glycolytic pathway associated with hereditary hemolytic anemia. History of discovery, clinical features, biochemical studies, as well as recent studies on molecular level were reviewed, with a stress on our own studies. As reference materials, Tables 2 and
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PK deficiency is the most common and well characterized erythroenzymopathy in the Embden-Meyerhof glycolytic pathway associated with hereditary hemolytic anemia. History of discovery, clinical features, biochemical studies, as well as recent studies on molecular level were reviewed, with a stress on our own studies. As reference materials, Tables 2 and
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Pyruvate kinase deficiency in children
Pediatric Blood & Cancer, 2021AbstractBackgroundPyruvate kinase deficiency (PKD) is a rare, autosomal recessive red blood cell enzyme disorder, which leads to lifelong hemolytic anemia and associated complications from the disease and its management.MethodsAn international, multicenter registry enrolled 124 individuals younger than 18 years old with molecularly confirmed PKD from ...
Rachael F. Grace+18 more
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Defective erythrocyte pyruvate kinase
Clinica Chimica Acta, 1976A defective pyruvate kinase (EC 2.7.1.40) is described. The abnormal PK is characterized by a shift in the R in equilibrium T equilibrium to the T-state. The Ko.5 for the substrate phosphoenol pyruvate is about 6 times higher than for the normal enzyme, while the KM value for the positive effector Fru-1, 6-P2 is increased.
A.M.C. Vlug+3 more
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Advances in Enzyme Regulation, 1969
Abstract The mechanism and sequence of events of the induction of liver pyruvate kinase by sucrose and fructose administration were examined. Actinomycin and cycloheximide prevented the sucrose and fructose induced rise in pyruvate kinase activity.
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Abstract The mechanism and sequence of events of the induction of liver pyruvate kinase by sucrose and fructose administration were examined. Actinomycin and cycloheximide prevented the sucrose and fructose induced rise in pyruvate kinase activity.
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Pyruvate kinase of Bacillus subtilis
Biochimica et Biophysica Acta (BBA) - Enzymology, 1972Abstract Conditions are reported which stabilize pyruvate kinase (ATP: pyruvate phosphotransferase, EC 2.7.1.40) activity in extracts of Bacillus subtilis. These conditions include high protein concentrations and the presence of KCl and phosphoenolpyruvate.
Martin D. Diesterhaft, Ernst Freese
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Pyruvate kinase of higher plants
Biochimica et Biophysica Acta (BBA) - General Subjects, 1973Abstract 1. 1. Pyruvate kinase (EC 2.7.1.40) was extracted from pea seeds and carrots and partially purified by fractionation with (NH4)2SO4. 2. 2. The enzyme from both sources showed hyperbolic kinetics for the substrates phosphoenolpyruvate and ADP. Mg2+ or Mn2+ and a movement cation were required for enzyme activity.
John F. Turner, J. David Tomlinson
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Radiotracer assay of pyruvate kinase
Analytical Biochemistry, 1971Abstract A radiotracer enzyme assay for the determination of pyruvate kinase activity is described. The rate of the enzyme catalyzed reaction is determined by radioassay of either ATP- 3 H formed or unreacted ADP- 3 H, or both after their separations from the assay reaction mixture by TLC.
Donald G. Therriault+1 more
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Relaxation spectra of pyruvate kinase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1970Relaxation studies using the temperature jump have been carried out on pyruvate kinase (ATP: pyruvate phosphotransferase, EC 2.7.1.40) isolated from rabbit muscle. Several concentration-independent relaxation effects with associated relaxation times of approx.
Gordon G. Hammes, Jon Simplicio
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2021
Pyruvate kinase is an important enzyme of glycolytic pathway that catalyzes the last step of this pathway. In human erythrocytes, there is no mitochondrion hence glycolytic pathway is the most important source of energy generation. In vitro, in vivo, and case control studies suggested that pyruvate kinase deficiency provides resistance against P ...
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Pyruvate kinase is an important enzyme of glycolytic pathway that catalyzes the last step of this pathway. In human erythrocytes, there is no mitochondrion hence glycolytic pathway is the most important source of energy generation. In vitro, in vivo, and case control studies suggested that pyruvate kinase deficiency provides resistance against P ...
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Pyruvate Kinase Deficiency and Malaria
New England Journal of Medicine, 2008Malaria that is caused by Plasmodium falciparum is a significant global health problem. Genetic characteristics of the host influence the severity of disease and the ultimate outcome of infection, and there is evidence of coevolution of the plasmodium parasite with its host.
Melanie Kirby-Allen+7 more
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