The enthalpy of protolysis of liver alcohol dehydrogenase upon binding nicotinamide adenine dinucleotide.

[1]  Lawson Wr,et al.  The mechanism of quenching of liver alcohol dehydrogenase fluorescence due to ternary complex formation. , 1978 .

[2]  C. Hanes,et al.  Parallelism between ethanol and imidazole interactions with horse liver alcohol dehydrogenase. , 1978, Canadian journal of biochemistry.

[3]  P. Luisi,et al.  Fluorescence quenching and energy transfer in complexes between horse-liver alcohol dehydrogenase and coenzymes. , 1978, European journal of biochemistry.

[4]  D. Sigman,et al.  Limiting rates of ligand association to alcohol dehydrogenase. , 1978, Archives of biochemistry and biophysics.

[5]  D. M. Parker,et al.  pH-dependent changes of intrinsic fluorescence of chemically modified liver alcohol dehydrogenases. , 1978, The Biochemical journal.

[6]  H. Eklund,et al.  Crystallography of liver alcohol dehydrogenase complexed with substrates. , 1978, Journal of molecular biology.

[7]  P. Ross,et al.  Thermodynamics of binding of oxidized and reduced nicotinamide adenine dinucleotides, adenosine-5'-diphosphoribose, and 5'-iodosalicylate to dehydrogenases. , 1978, Biochemistry.

[8]  C. Branden,et al.  The crystal structure of complexes between horse liver alcohol dehydrogenase and the coenzyme analogues 3-iodopyridine-adenine dinucleotide and pyridine-adenine dinucleotide. , 1977, European journal of biochemistry.

[9]  P. Ross,et al.  Calorimetric investigation of NAD binding to some dehydrogenases. , 1977, Biochemical and biophysical research communications.

[10]  C. Brändén,et al.  X-ray investigation of the binding of 1,10-phenanthroline and imidazole to horse-liver alcohol dehydrogenase. , 1977, European journal of biochemistry.

[11]  C. Brändén Coenzyme-induced conformational changes and subunit interactions of liver alcohol dehydrogenase. , 1977, Biochemical Society transactions.

[12]  M. Dunn,et al.  Liver alcohol dehydrogenase-coenzyme reaction rates. , 1977, The Journal of biological chemistry.

[13]  K. Mosbach,et al.  Studies on conformation of soluble and immobilized enzymes using differential scanning calorimetry. 1. Thermal stability of nicotinamide adenine dinucleotide dependent dehydrogenases. , 1977, Biochemistry.

[14]  B. Geiger,et al.  Immunochemical determination of tubulin , 1977, FEBS letters.

[15]  D. Shiao,et al.  Heats of binding protons to globular proteins , 1976, Biopolymers.

[16]  P. Woolley Models for metal ion function in carbonic anhydrase , 1975, Nature.

[17]  H. Jörnvall,et al.  Carboxymethylation of horse-liver alcohol dehydrogenase in the crystalline state. The active-site zinc region and general anion-binding site of the enzyme correlated in primary and teritiary structures. , 1975, European journal of biochemistry.

[18]  C. Reynolds,et al.  Carboxymethyl horse-liver alcohol dehydrogenase. Ligand-binding and kinetic properties of the cysteine-46-modified enzyme. , 1975, Archives of biochemistry and biophysics.

[19]  H. Eklund,et al.  3 Alcohol Dehydrogenases , 1975 .

[20]  H. Weiner,et al.  Role of zinc in horse liver alcohol dehydrogenase. Coenzyme and substrate binding. , 1972, Biochemistry.

[21]  H. Theorell,et al.  Dissociation constants of the binary complex of homogeneous horse liver alcohol dehydrogenase and nicotiniumamide adenine dinucleotide. , 1967, Acta chemica Scandinavica.

[22]  K. Dalziel KINETIC STUDIES OF LIVER ALCOHOL DEHYDROGENASE AND PH EFFECTS WITH COENZYME PREPARATIONS OF HIGH PURITY. , 1963, The Journal of biological chemistry.

[23]  H. Theorell,et al.  Liver Alcohol Dehydrogenase. III. Kinetics in the Presence of Caprate, Isobutyramide and Imidazole. , 1961 .

[24]  H. Theorell,et al.  Liver Alcohol Dehydrogenase. II. Equilibrium Constants of Binary and Ternary Complexes of Enzyme, Coenzyme, and Caprate, Isobutyramide and Imidazole. , 1961 .