NMR methods for measuring enzyme kinetics in vivo

[1]  G. Radda,et al.  31P-NMR saturation transfer measurements of exchange between Pi and ATP in the reactions catalysed by glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase in vitro. , 1987, Biochimica et biophysica acta.

[2]  G. Radda,et al.  31P nuclear-magnetic resonance saturation transfer measurements of flux between inorganic phosphate and ATP in yeast cells over-producing phosphoglycerate kinase , 1986 .

[3]  D. J. Hayes,et al.  One-dimensional rotating-frame imaging of phosphorus metabolites in vivo , 1986 .

[4]  G K Radda,et al.  The use of NMR spectroscopy for the understanding of disease. , 1986, Science.

[5]  I. Campbell,et al.  A 1H-NMR study of the activity expressed by lactate dehydrogenase in the human erythrocyte. , 1986, European journal of biochemistry.

[6]  D. Doddrell,et al.  Preliminary studies on the potential of in vivo deuterium NMR spectroscopy. , 1986, Biochemical and biophysical research communications.

[7]  G. M. Smith,et al.  NMR studies of [1-2H]glucose metabolism in Zymomonas mobilis. , 1986, European journal of biochemistry.

[8]  James E. Roberts,et al.  Nitrogen metabolism in Methanobacterium thermoautotrophicum: a solution and solid-state nitrogen-15 NMR study , 1986 .

[9]  A. From,et al.  31P NMR measurement of ATP synthesis rate in perfused intact rat hearts , 1986, FEBS letters.

[10]  P. Kuchel,et al.  Direct NMR evidence that prolidase is specific for the trans isomer of imidodipeptide substrates. , 1986, Biochemistry.

[11]  H. Kacser,et al.  Kinetics of metabolic pathways. A system in vitro to study the control of flux. , 1986, The Biochemical journal.

[12]  H. Kalbitzer,et al.  Observation of Mg2+.ATP and uncomplexed ATP in slow exchange by 31P-NMR at high magnetic fields. , 1986, Biochemical and biophysical research communications.

[13]  K Uğurbil,et al.  Measurement of an individual rate constant in the presence of multiple exchanges: application to myocardial creatine kinase reaction. , 1986, Biochemistry.

[14]  K. Uğurbil,et al.  Studies of anaerobic and aerobic glycolysis in Saccharomyces cerevisiae. , 1986, Biochemistry.

[15]  R. Shulman,et al.  Studies on the regulation of yeast phosphofructo-1-kinase: its role in aerobic and anaerobic glycolysis. , 1986, Biochemistry.

[16]  P. Kuchel,et al.  Direct quantitative analysis of enzyme-catalyzed reactions by two-dimensional nuclear magnetic resonance spectroscopy: adenylate kinase and phosphoglyceromutase , 1986 .

[17]  W. E. Jacobus.  Theoretical support for the heart phosphocreatine energy transport shuttle based on the intracellular diffusion limited mobility of ADP. , 1985, Biochemical and biophysical research communications.

[18]  K. Brindle,et al.  31P-NMR saturation transfer measurements of phosphate consumption in Saccharomyces cerevisiae , 1985 .

[19]  R. Shulman,et al.  In vivo 31P nuclear magnetic resonance saturation transfer measurements of phosphate exchange reactions in the yeast Saccharomyces cerevisiae , 1985, FEBS letters.

[20]  M. Weiner,et al.  Detection of Exchange Reactions Involving Small Metabolite Pools Using NMR Magnetization Transfer Techniques: Relevance to Subcellular Compartmentation of Creatine Kinase , 1985, Magnetic resonance in medicine.

[21]  D. J. Hayes,et al.  Biochemical adaptation in the skeletal muscle of rats depleted of creatine with the substrate analogue beta-guanidinopropionic acid. , 1985, The Biochemical journal.

[22]  E. Shoubridge,et al.  Creatine kinase kinetics, ATP turnover, and cardiac performance in hearts depleted of creatine with the substrate analogue beta-guanidinopropionic acid. , 1985, Biochimica et Biophysica Acta.

[23]  R. Shulman,et al.  Kinetics of creatine kinase in heart: a 31P NMR saturation- and inversion-transfer study. , 1985, Biochemistry.

[24]  K. Uğurbil.  Magnetization-transfer measurements of individual rate constants in the presence of multiple reactions , 1985 .

[25]  P. Kuchel,et al.  Regulation of the human-erythrocyte hexose-monophosphate shunt under conditions of oxidative stress: a study using NMR spectroscopy, a kinetic isotope effect, a reconstituted system and computer simulation , 1985 .

[26]  G. Radda,et al.  Measurements of exchange in the reaction catalysed by creatine kinase using 14C and 15N isotope labels and the NMR technique of saturation transfer. , 1985, Biochimica et biophysica acta.

[27]  J. Ingwall,et al.  Reaction rates of creatine kinase and ATP synthesis in the isolated rat heart. A 31P NMR magnetization transfer study. , 1985, The Journal of biological chemistry.

[28]  A. Cornish-Bowden,et al.  Control analysis of metabolic systems , 1985 .

[29]  V A Saks,et al.  Regulation of energy flux through the creatine kinase reaction in vitro and in perfused rat heart. 31P-NMR studies. , 1984, Biochimica et biophysica acta.

[30]  I. Campbell,et al.  A comparison of one-dimensional and two-dimensional NMR methods for measuring enzyme-catalyzed exchange , 1984 .

[31]  R. Shulman,et al.  Carbon-13 nuclear magnetic resonance studies of myocardial glycogen metabolism in live guinea pigs. , 1984, Biochemistry.

[32]  E. Shoubridge,et al.  A 31P-nuclear magnetic resonance study of skeletal muscle metabolism in rats depleted of creatine with the analogue beta-guanidinopropionic acid. , 1984, Biochimica et biophysica acta.

[33]  I. Campbell,et al.  A multinuclear NMR study of 2,3-bisphosphoglycerate metabolism in the human erythrocyte. , 1984, Biochimica et biophysica acta.

[34]  E. Shoubridge,et al.  Regulation of creatine kinase during steady-state isometric twitch contraction in rat skeletal muscle. , 1984, Biochimica et biophysica acta.

[35]  R. Balaban,et al.  Kinetics of creatine phosphokinase and adenylate kinase. A two-dimensional NMR analysis. , 1984, Biochimica et biophysica acta.

[36]  P W Kuchel,et al.  31P NMR spin-transfer in the phosphoglyceromutase reaction. , 1984, European journal of biochemistry.

[37]  Walter J. Moore,et al.  Skewed exchange spectroscopy. Two-dimensional method for the measurement of cross relaxation in proton NMR spectroscopy , 1984 .

[38]  C. Perrin,et al.  Multisite kinetics by quantitative two-dimensional NMR , 1984 .

[39]  G. T. Rich,et al.  Glyceraldehyde-3-phosphate dehydrogenase release from erythrocytes during haemolysis. No evidence for substantial binding of the enzyme to the membrane in the intact cell. , 1984, The Biochemical journal.

[40]  I. Campbell,et al.  The inhibition of erythrocyte glyceraldehyde-3-phosphate dehydrogenase. In situ PMR studies. , 1984, Biochimica et biophysica acta.

[41]  D. Doddrell,et al.  In vivo proton NMR spectroscopy , 1984 .

[42]  G. Radda,et al.  A comparison of 31P-NMR saturation transfer and isotope-exchange measurements of creatine kinase kinetics in vitro. , 1984, Biochimica et biophysica acta.

[43]  O. Jardetzky,et al.  Measurement of mitochondrial ATPase activity in maize root tips by saturation transfer p nuclear magnetic resonance. , 1984, Plant physiology.

[44]  B. Nageswara Rao,et al.  Analysis of 31P NMR spectra of enzyme-bound reactants and products of adenylate kinase using density matrix theory of chemical exchange. , 1984, Biochemistry.

[45]  I. Campbell,et al.  1H NMR measurements of enzyme-catalyzed 15N-label exchange , 1984 .

[46]  R G Shulman,et al.  NMR studies of enzymatic rates in vitro and in vivo by magnetization transfer , 1984, Quarterly Reviews of Biophysics.

[47]  J. Sanders,et al.  Formaldehyde metabolism by Escherichia coli. In vivo carbon, deuterium, and two-dimensional NMR observations of multiple detoxifying pathways. , 1984, Biochemistry.

[48]  H. Westerhoff,et al.  Modern theories of metabolic control and their applications , 1984, Bioscience reports.

[49]  S. Cohen.  Simultaneous 13C and 31P NMR studies of perfused rat liver. Effects of insulin and glucagon and a 13C NMR assay of free Mg2+. , 1983, The Journal of biological chemistry.

[50]  E M Chance,et al.  Mathematical analysis of isotope labeling in the citric acid cycle with applications to 13C NMR studies in perfused rat hearts. , 1983, The Journal of biological chemistry.

[51]  I. Campbell,et al.  Proton NMR measurements of hydrogen exchange at the C‐3 position of 3‐hydroxybutyrate in suspensions of rat liver mitochondria , 1983, FEBS letters.

[52]  R. Balaban,et al.  In vivo flux between phosphocreatine and adenosine triphosphate determined by two-dimensional phosphorous NMR. , 1983, The Journal of biological chemistry.

[53]  H. Kacser,et al.  Enzyme variation, metabolic flux and fitness: alcohol dehydrogenase in Drosophila melanogaster. , 1983, Genetics.

[54]  P. J Hors,et al.  A new method for water suppression in the proton NMR spectra of aqueous solutions , 1983 .

[55]  G. Radda,et al.  Energetics of sodium transport in the kidney. Saturation transfer 31P-NMR. , 1983, Biochimica et biophysica acta.

[56]  P. Garlick,et al.  The application of phosphorus two-dimensional NMR exchange spectroscopy to cardiac metabolism , 1983 .

[57]  J. S. Cohen,et al.  Selective observation of 13C-enriched metabolites by 1H NMR , 1983 .

[58]  I. Campbell,et al.  Observation of carbon labelling in cell metabolites using proton spin echo NMR. , 1982, Biochemical and biophysical research communications.

[59]  I. Campbell,et al.  A 1H n.m.r. study of the kinetic properties expressed by glyceraldehyde phosphate dehydrogenase in the intact human erythrocyte. , 1982, The Biochemical journal.

[60]  D. Gadian,et al.  A 31P-NMR saturation transfer study of the regulation of creatine kinase in the rat heart. , 1982, Biochimica et biophysica acta.

[61]  I. Campbell,et al.  Spin ECHO proton NMR studies of the metabolism of malate and fumarate in human erythrocytes. Dependence on free NAD levels. , 1982, Biochimica et biophysica acta.

[62]  S. Ogawa,et al.  A study on the exchange rate of magnesium with ATP. , 1982, Biochimica et biophysica acta.

[63]  P. Kuchel,et al.  Incorporation of labelled glycine into reduced glutathione of intact human erythrocytes by enzyme-catalysed exchange. A nuclear-magnetic-resonance study. , 1982, The Biochemical journal.

[64]  E. Schaftingen,et al.  Fructose 2,6-bisphosphate 2 years after its discovery. , 1982, The Biochemical journal.

[65]  R. Shulman,et al.  In vivo phosphorus-31 nuclear magnetic resonance saturation transfer studies of adenosinetriphosphatase kinetics in Saccharomyces cerevisiae. , 1982, Biochemistry.

[66]  C. Dobson,et al.  Time development of proton nuclear overhauser effects in proteins , 1982 .

[67]  E. Shoubridge,et al.  31P NMR saturation transfer measurements of the steady state rates of creatine kinase and ATP synthetase in the rat brain , 1982, FEBS letters.

[68]  H. Westerhoff,et al.  Quantification of the contribution of various steps to the control of mitochondrial respiration. , 1982, The Journal of biological chemistry.

[69]  I. Campbell,et al.  A p.m.r. isotope-exchange method for studying the kinetic properties of dehydrogenases in intact cells. , 1982, The Biochemical journal.

[70]  I. Campbell,et al.  A 1H n.m.r. study of isotope exchange catalysed by glycolytic enzymes in the human erythrocyte. , 1982, The Biochemical journal.

[71]  I. Campbell,et al.  Studies of lactate dehydrogenase in the purified state and in intact erythrocytes. , 1982, The Biochemical journal.

[72]  Richard R. Ernst,et al.  Direct determination of rate constants of slow dynamic processes by two-dimensional \"accordion\" spectroscopy in nuclear magnetic resonance , 1982 .

[73]  V. Kollman,et al.  13C nuclear magnetic resonance studies of the biosynthesis by Microbacterium ammoniaphilum of L-glutamate selectively enriched with carbon-13. , 1982, The Journal of biological chemistry.

[74]  A. N. Stevens,et al.  NMR Studies of metabolites in living tissue , 1982 .

[75]  D. Gadian,et al.  The steady-state rate of ATP synthesis in the perfused rat heart measured by 31P NMR saturation transfer. , 1981, Biochemical and biophysical research communications.

[76]  H. Kacser,et al.  Control of the flux in the arginine pathway of Neurospora crassa. Modulations of enzyme activity and concentration. , 1981, The Biochemical journal.

[77]  O Jardetzky,et al.  Monitoring of cellular metabolism by NMR. , 1981, Biochimica et biophysica acta.

[78]  R. Shulman,et al.  High-resolution proton NMR studies of intracellular metabolites in yeast using 13C decoupling☆ , 1981 .

[79]  T. Takala,et al.  Effect of Mechanical Work Load on the Transmural Distribution of Glucose Uptake in the Isolated Perfused Rat Heart, Studied by Regional Deoxyglucose Trapping , 1981, Circulation research.

[80]  R. Shulman,et al.  A comparison of 13C nuclear magnetic resonance and 14C tracer studies of hepatic metabolism. , 1981, The Journal of biological chemistry.

[81]  T. Mareci,et al.  Weak satellite signals in high-resolution NMR spectra: Separating the wheat from the chaff , 1981 .

[82]  D. Doddrell,et al.  NMR OF PROTONS COUPLED TO CARBON-13 NUCLEI ONLY , 1981 .

[83]  P J Geiger,et al.  Transport of energy in muscle: the phosphorylcreatine shuttle. , 1981, Science.

[84]  D. Wilkie,et al.  The activity of creatine kinase in frog skeletal muscle studied by saturation-transfer nuclear magnetic resonance. , 1981, The Biochemical journal.

[85]  P. Bottomley,et al.  Assessment of pharmacological treatment of myocardial infarction by phosphorus-31 NMR with surface coils. , 1981, Science.

[86]  G K Radda,et al.  NMR studies of tissue metabolism. , 1981, Annual review of biochemistry.

[87]  T. Ogino,et al.  Proton correlation nuclear magnetic resonance study of metabolic regulations and pyruvate transport in anaerobic Escherichia coli cells. , 1980, Biochemistry.

[88]  H. Kliman,et al.  Association of glyceraldehyde-3-phosphate dehydrogenase with the human red cell membrane. A kinetic analysis. , 1980, The Journal of biological chemistry.

[89]  H. Sies.  From enzymology in vitro to physiological chemistry in vivo , 1980 .

[90]  W. Cleland.  Measurement of isotope effects by the equilibrium perturbation technique. , 1980, Methods in enzymology.

[91]  C. Dobson,et al.  The application of high resolution nuclear magnetic resonance to biological systems. , 2006, Methods of biochemical analysis.

[92]  G K Radda,et al.  Studies of acidosis in the ischaemic heart by phosphorus nuclear magnetic resonance. , 1979, The Biochemical journal.

[93]  Richard R. Ernst,et al.  Investigation of exchange processes by two‐dimensional NMR spectroscopy , 1979 .

[94]  R. Shulman,et al.  Phosphorus-31 nuclear magnetic resonance studies of wild-type and glycolytic pathway mutants of Saccharomyces cerevisiae. , 1979, Biochemistry.

[95]  R. Nunnally,et al.  Adenosine triphosphate compartmentation in living hearts: a phosphorus nuclear magnetic resonance saturation transfer study. , 1979, Biochemistry.

[96]  Raj K. Gupta.  Saturation transfer 31P NMR studies of the intact human red blood cell , 1979 .

[97]  H A Krebs,et al.  Cytosolic phosphorylation potential. , 1979, The Journal of biological chemistry.

[98]  T R Brown,et al.  Cellular applications of 31P and 13C nuclear magnetic resonance. , 1979, Science.

[99]  P W Kuchel,et al.  Application of spin-echo nuclear magnetic resonance to whole-cell systems. Membrane transport. , 1979, The Biochemical journal.

[100]  N. Carr.  Studies in microbiology , 1979 .

[101]  O. H. Lowry,et al.  Enzyme patterns in single human muscle fibers. , 1978, The Journal of biological chemistry.

[102]  J. Meeks,et al.  Formation of glutamine from [13n]ammonia, [13n]dinitrogen, and [14C]glutamate by heterocysts isolated from Anabaena cylindrica , 1977, Journal of bacteriology.

[103]  C. Masters.  Metabolic control and the microenvironment. , 1977, Current topics in cellular regulation.

[104]  J. Ottaway,et al.  The role of compartmentation in the control of glycolysis. , 1977, Current topics in cellular regulation.

[105]  D. Hoult.  Solvent peak saturation with single phase and quadrature fourier transformation , 1976 .

[106]  I. R. Peat,et al.  The experimental approach to accurate carbon-13 spin-lattice relaxation measurements , 1975 .

[107]  Reinhart Heinrich,et al.  A linear steady-state treatment of enzymatic chains. General properties, control and effector strength. , 1974, European journal of biochemistry.

[108]  N. Matwiyoff,et al.  Carbon-13 NMR spectroscopy of red blood cell suspensions. , 1972, Biochemical and biophysical research communications.

[109]  F. S. Rolleston.  A Theoretical Background to the Use of Measured Concentrations of Intermediates in Study of the Control of Intermediary Metabolism , 1972 .

[110]  A. Sols,et al.  Concentrations of Metabolites and Binding Sites. Implications in Metabolic Regulation , 1970 .

[111]  G. Yagil,et al.  Rate of isotope exchange in enzyme-catalyzed reactions. , 1969, Biochemistry.

[112]  D G Rhoads,et al.  Initial velocity and equilibrium kinetics of myokinase. , 1968, The Journal of biological chemistry.

[113]  P. Boyer,et al.  EQUILIBRIUM REACTION RATES AND THE MECHANISMS OF BOVINE HEART AND RABBIT MUSCLE LACTATE DEHYDROGENASES. , 1964, The Journal of biological chemistry.

[114]  S. Forsén,et al.  Study of Moderately Rapid Chemical Exchange Reactions by Means of Nuclear Magnetic Double Resonance , 1963 .

[115]  H. Mcconnell.  Reaction Rates by Nuclear Magnetic Resonance , 1958 .