Structure and function of haemoglobin.

[1]  C. Ho,et al.  Effects of ligands and organic phosphates on functional properties of human adult hemoglobin. , 1974, Biochemistry.

[2]  J E Ladner,et al.  Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin. , 1974, Biochemistry.

[3]  J E Ladner,et al.  Influence of globin structure on the state of the heme. 3. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction. , 1974, Biochemistry.

[4]  A. Fersht,et al.  Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin. , 1974, Biochemistry.

[5]  M. Perutz,et al.  Structure of inositol hexaphosphate–human deoxyhaemoglobin complex , 1974, Nature.

[6]  J. Kilmartin.  Influence of DPG on the bohr effect of human hemoglobin , 1974 .

[7]  R. Noble,et al.  The effect of inositol hexaphosphate on the allosteric properties of carp hemoglobin. , 1973, The Journal of biological chemistry.

[8]  L. Rossi-Bernardi,et al.  Role of the α-Amino Groups of the α and β Chains of Human Hemoglobin in Oxygen-linked Binding of Carbon Dioxide , 1973 .

[9]  C. Ho,et al.  Nuclear magnetic resonance and spin-label studies of hemoglobin Kempsey. , 1973, Biochemistry.

[10]  S. Rapoport,et al.  Interaction of Haemoglobin with Ions , 1973 .

[11]  K. Moffat,et al.  The Ligand-binding Properties of desHis(146β) Hemoglobin , 1973 .

[12]  L Anderson,et al.  Intermediate structure of normal human haemoglobin: methaemoglobin in the deoxy quaternary conformation. , 1973, Journal of molecular biology.

[13]  A. Riggs,et al.  Kinetic and equilibrium properties of hemoglobin Kansas. , 1973, The Journal of biological chemistry.

[14]  J. Kilmartin.  The interaction of inositol hexaphosphate with methaemoglobin. , 1973, The Biochemical journal.

[15]  J J Hopfield,et al.  Relation between structure, co-operativity and spectra in a model of hemoglobin action. , 1973, Journal of molecular biology.

[16]  M. Raftery,et al.  Characterization of intermediate states in the ligation of hemoglobin. , 1973, Biochemistry.

[17]  K. Imai,et al.  PH dependence of the shape of the hemoglobin-oxygen equilibrium curve. , 1973, Biochimica et biophysica acta.

[18]  M. Brunori,et al.  Kinetics of the reaction between oxygen and haemoglobin bound to haptoglobin. , 1973, The Biochemical journal.

[19]  R. Noble,et al.  Conditions restricting allosteric transitions in carp hemoglobin. , 1973, The Journal of biological chemistry.

[20]  K. Imai,et al.  Analysis of oxygen equilibrium of hemoglobin and control mechanism of organic phosphates. , 1973, Biochemistry.

[21]  Q. Gibson,et al.  Ligand binding kinetics of des arginine haemoglobin. , 1973, Journal of molecular biology.

[22]  R. Nagel,et al.  The binding of 2,3-diphosphoglycerate as a conformational probe of human hemoglobins. , 1973, Journal of molecular biology.

[23]  Q. Gibson,et al.  The Effects of pH and Anions on the Properties of the α and β Chains within Human Deoxyhemoglobin , 1973 .

[24]  Q. Gibson,et al.  The release of protons and anions during ligand binding to human deoxyhemoglobin. , 1973, The Journal of biological chemistry.

[25]  J. Karle,et al.  Crystal structure analysis of sea lamprey hemoglobin at 2 Å resolution , 1973 .

[26]  D. Aitken.  Infrared in Space , 1973, Nature.

[27]  K. Imai.  Analyses of oxygen equilibria of native and chemically modified human adult hemoglobins on the basis of Adair's stepwise oxygenation theory and the allosteric model of Monod, Wyman, and Changeux. , 1973, Biochemistry.

[28]  Q. Gibson.  p-Mercuribenzoate as an indicator of conformation change in hemoglobin. , 1973, The Journal of biological chemistry.

[29]  Non-linear relationships between oxygen saturation and magnitude of fine structure of ultraviolet oxy versus deoxy difference spectrum in human hemoglobin. , 1973, Biochemical and biophysical research communications.

[30]  P. Pulsinelli.  Structure of deoxyhaemoglobin Yakima: a high-affinity mutant form exhibiting oxy-like 1 2 subunit interactions. , 1973, Journal of molecular biology.

[31]  Y. Henry,et al.  Reciprocal effects of change of subunit structure on ligand equilibria of haemoglobin valency hybrids. Attempted correlation with electron paramagnetic resonance spectra. , 1973, Journal of molecular biology.

[32]  M. Rabinowitz,et al.  Comparison of the mitochondrial ribonucleic acid from a wild-type grande and a cytoplasmic peptide yeast by ribonucleic acid-deoxyribonucleic acid hybridization. , 1973, Biochemistry.

[33]  S. Edelstein,et al.  Observation of the dissociation of unliganded hemoglobin. , 1972, The Journal of biological chemistry.

[34]  S. Ogawa,et al.  High resolution proton magnetic resonance study of the two quaternary states in fully ligated hemoglobin Kansas. , 1972, Biochemical and biophysical research communications.

[35]  J. Hopfield,et al.  The rate of carbon monoxide binding to hemoglobin Kansas. , 1972, Biochemical and biophysical research communications.

[36]  M Karplus,et al.  A mathematical model for structure-function relations in hemoglobin. , 1972, Journal of molecular biology.

[37]  R. Nagel,et al.  The ligand-binding properties of hemoglobin Hiroshima ( 2 2 146asp ). , 1972, The Journal of biological chemistry.

[38]  S. Edelstein,et al.  Cat Hemoglobin: pH-Dependent Cooperativity of Oxygen Binding , 1972, Science.

[39]  M. Raftery,et al.  19 F-NMR studies of oxygen binding to hemoglobin. , 1972, Biochemical and biophysical research communications.

[40]  Q. Gibson,et al.  The kinetics of ligand binding to hemoglobin valency hybrids and the effect of anions. , 1972, The Journal of biological chemistry.

[41]  R. S. Eliot,et al.  The deoxygenation kinetics of hemoglobin partially saturated with carbon monoxide. Effect of 2,3-diphosphoglycerate. , 1972, The Journal of biological chemistry.

[42]  M. Raftery,et al.  31 P-NMR studies of the release of diphospholygeric acid on carbon monoxide binding to hemoglobin. , 1972, Biochemical and biophysical research communications.

[43]  J. Wyman,et al.  Nuclear magnetic resonance quadrupole relaxation studies of chloride binding to human oxy- and deoxyhaemoglobin. , 1972, Journal of molecular biology.

[44]  G. Geraci,et al.  Reactivity of the 93 sulphydryls of human haemoglobin A: influence of the C-terminal residues. , 1972, Journal of molecular biology.

[45]  S. Ogawa,et al.  High resolution nuclear magnetic resonance spectra of hemoglobin: II. Ligated tetramers , 1972 .

[46]  S. Ogawa,et al.  High resolution nuclear magnetic resonance spectra of hemoglobin: I. The cyanide complexes of α and β chains , 1972 .

[47]  R G Shulman,et al.  High resolution nuclear magnetic resonance spectra of hemoglobin: III. The half-ligated state and allosteric interactions , 1972 .

[48]  K. Imai,et al.  Effects of 2,3-diphosphoglycerate on the oxygen equilibria of the half-cyanmet hybrid hemoglobins. , 1972, Biochemistry.

[49]  Q. Gibson,et al.  Ligand binding and release of an analogue of 2,3-diphosphoglycerate from human hemoglobin. , 1972, The Journal of biological chemistry.

[50]  N. Maeda,et al.  Affinity labeling of the polyphosphate binding site of hemoglobin. , 1972, Biochemistry.

[51]  R. Nagel,et al.  The hemoglobin-haptoglobin reaction as a probe of hemoglobin conformation. , 1972, Biochemical and biophysical research communications.

[52]  T. Asakura.  Non-linear relation between oxygen-binding and structural changes of hemoglobin. , 1972, Biochemical and biophysical research communications.

[53]  W. Huestis,et al.  The binding of n-butyl isocyanide to human hemoglobin. , 1972, Biochemical and biophysical research communications.

[54]  Judith Herzfeld,et al.  A general model of cooperativity and its application to DPG inhibition of hemoglobin oxygenation. , 1972, Biochemical and biophysical research communications.

[55]  M. McDonald,et al.  The effect of pH on the rates of ligand replacement reactions of human adult and fetal hemoglobins and their subunits. , 1972, The Journal of biological chemistry.

[56]  J. Hopfield,et al.  An allosteric model of hemoglobin. II. The assumption of independent binding. , 1972, Archives of biochemistry and biophysics.

[57]  M. F. Perutz,et al.  Nature of Haem–Haem Interaction , 1972, Nature.

[58]  C. Ho,et al.  Nuclear magnetic resonance studies of haemoglobin M Milwaukee. , 1972, Nature: New biology.

[59]  Q. Gibson,et al.  The functional properties of hemoglobin Bethesda ( 2 2 145His ). , 1972, The Journal of biological chemistry.

[60]  A. Arnone.  X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin , 1972, Nature.

[61]  C. Ho,et al.  Nuclear magnetic resonance studies of hemoglobins. VII. Tertiary structure around ligand binding site in carbonmonoxyhemoglobin. , 1972, Biochemistry.

[62]  M. Raftery,et al.  A study of cooperative interactions in hemoglobin using fluorine nuclear magnetic resonance. , 1972, Biochemistry.

[63]  G. Guidotti,et al.  Stabilizing interactions in hemoglobin. , 1972, The Journal of biological chemistry.

[64]  H. Mcconnell,et al.  Binding of triphosphate spin labels to hemoglobin Kempsey. , 1972, Biochemical and biophysical research communications.

[65]  M. Brunori,et al.  Studies on the reaction of isocyanides with haemproteins. II. Binding to normal and modified human haemoglobins. , 1972, Journal of molecular biology.

[66]  O. Siggaard‐Andersen,et al.  Oxygen-linked hydrogen ion binding of human hemoglobin. Effects of carbon dioxide and 2,3-diphosphoglycerate. , 1972, Scandinavian journal of clinical and laboratory investigation.

[67]  Q. Gibson,et al.  The reaction of n-butyl isocyanide with human hemoglobin. II. The ligand-binding properties of the and chains within deoxyhemoglobin. , 1972, The Journal of biological chemistry.

[68]  H. Fasold,et al.  On the kinetics of the reaction of hemoglobin with CO. Flash-photolysis experiments. , 1972, European journal of biochemistry.

[69]  M. Brunori,et al.  Properties of the product of partial photodissociation of carbon monoxide hemoglobin. , 1972, The Journal of biological chemistry.

[70]  K. Imai,et al.  Physicochemical studies of the relation between structure and function in hemoglobin Hiroshima (HC3 , histidine leads to aspartate). , 1972, Biochemistry.

[71]  Enhancement of the Acid and Alkaline Bohr Effects of Hemoglobin by Organic Phosphates , 1972 .

[72]  J L Hoard,et al.  Stereochemistry of hemes and other metalloporphyrins. , 1971, Science.

[73]  Q. Gibson,et al.  The effect of inositol hexaphosphate on the kinetics of CO and O 2 binding by human hemoglobin. , 1971, The Journal of biological chemistry.

[74]  G. Kellett.  Ligand-free haemoglobin dimers. , 1971, Nature: New biology.

[75]  W. Gratzer,et al.  Cofactor binding and oxygen equilibria in haemoglobin. , 1971, Nature: New biology.

[76]  J. Greer.  Three-dimensional structure of abnormal human haemoglobins Chesapeake and J Capetown. , 1971, Journal of molecular biology.

[77]  J. Hopfield,et al.  An allosteric model of hemoglobin. I. Kinetics. , 1971, Journal of molecular biology.

[78]  L. Janssen,et al.  Effect of 2,3-diphosphoglycerate on the Bohr effect of human adult hemoglobin. , 1971, Biochemical and biophysical research communications.

[79]  Q. Gibson,et al.  The dissociation of the first oxygen molecule from some mammalian oxyhemoglobins. , 1971, The Journal of biological chemistry.

[80]  C. Ho,et al.  Nuclear magnetic resonance studies of hemoglobins. 8. Evidence for preferential ligand binding to chains within deoxyhemoglobins. , 1971, Biochemical and biophysical research communications.

[81]  Q. Gibson,et al.  The reaction of n-butyl isocyanide with human hemoglobin. I. Determination of the kinetic parameters involved in the last step in ligand binding. , 1971, The Journal of biological chemistry.

[82]  S. Ogawa,et al.  Effects of phosphate upon CO binding kinetics and NMR spectra of hemoglobin valency hybrids. , 1971, Biochemical and biophysical research communications.

[83]  D. G. Davis,et al.  Nuclear magnetic resonance studies of hemoglobins. VI. Heme proton spectra of human deoxyhemoglobins and their relevance to the nature of co-operative oxygenation of hemoglobin. , 1971, Journal of molecular biology.

[84]  Q. Gibson,et al.  The binding of carbon monoxide to and chains in tetrameric mammalian hemoglobin. , 1971, The Journal of biological chemistry.

[85]  H. K. Schachman,et al.  Dissociation of hemoglobin into subunits. Monomer formation and the influence of ligands. , 1971, Journal of molecular biology.

[86]  G. Kellett.  Dissociation of hemoglobin into subunits. Ligand-linked dissociation at neutral pH. , 1971, Journal of molecular biology.

[87]  M. Perutz,et al.  Haemoglobin Hiroshima and the mechanism of the alkaline Bohr effect. , 1971, Nature: New biology.

[88]  L. Rossi-Bernardi,et al.  The binding of carbon dioxide by horse haemoglobin. , 1971, The Biochemical journal.

[89]  J. Greer.  Three-dimensional structure of abnormal human haemoglobins M Hyde Park and M Iwate. , 1971, Journal of molecular biology.

[90]  J. Greer.  Three-dimensional structure of abnormal human haemoglobins Kansas and Richmond. , 1971, Journal of molecular biology.

[91]  R. Nagel,et al.  Ligand binding in hemoglobin J Capetown. , 1971, Journal of molecular biology.

[92]  J. K. Moffat.  Structure and functional properties of chemically modified horse hemoglobin. II. X-ray studies. , 1971, Journal of molecular biology.

[93]  M. Brunori,et al.  Studies on the reaction of isocyanides with haemproteins. I. Equilibria and kinetics of the binding to the isolated chains of human haemoglobin. , 1971, Journal of molecular biology.

[94]  W. Konigsberg,et al.  Structure and functional properties of chemically modified horse hemoglobin. I. Determination of the functional properties. , 1971, Journal of molecular biology.

[95]  Gibson Qh,et al.  The kinetics of ligand binding and of the association-dissociation reactions of human hemoglobin. Properties of deoxyhemoglobin dimers. , 1971 .

[96]  J. Adamson,et al.  Haemoglobin Rainier : β145 (HC2) Tyrosine→Cysteine and Haemoglobin Bethesda: β145 (HC2) Tyrosine → Histidine , 1971 .

[97]  M. Perutz,et al.  Three dimensional structure of haemoglobin Rainier. , 1971, Nature: New biology.

[98]  K. Imai,et al.  Effect of 2,3-diphosphoglycerate on the cooperativity in oxygen binding of human adult hemoglobin. , 1971, Biochemical and biophysical research communications.

[99]  T. Maeda,et al.  Kinetic evidence for propagation of conformational changes in the alpha subunit to the beta subunit of hemoglobin. , 1971, Biochemistry.

[100]  S. Edelstein.  Extensions of the Allosteric Model for Haemoglobin , 1971, Nature.

[101]  A. Riggs,et al.  Studies of the interaction of 2,3-diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant. , 1971, The Journal of biological chemistry.

[102]  J. K. Moffat.  Spin-labelled haemoglobins: a structural interpretation of electron paramagnetic resonance spectra based on X-ray analysis. , 1971, Journal of molecular biology.

[103]  Q. Gibson,et al.  Functional Heterogeneity of the α and β Chains in the Oxidation-Reduction Reaction of Human Hemoglobin , 1971 .

[104]  S. Ogawa,et al.  Observation of allosteric transition in hemoglobin. , 1971, Biochemical and biophysical research communications.

[105]  M. Brunori,et al.  Enzyme Proteins. (Book Reviews: Hemoglobin and Myoglobin in Their Reactions with Ligands) , 1971 .

[106]  J. Kilmartin,et al.  Inhibition of Bohr Effect after Removal of C-Terminal Histidines from Haemoglobin β-Chains , 1970, Nature.

[107]  M. Perutz.  Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery , 1970, Nature.

[108]  M. F. PERUTZ,et al.  Three Dimensional Fourier Synthesis of Horse Deoxyhaemoglobin at 2.8 Å Resolution , 1970, Nature.

[109]  H. Muirhead,et al.  Three-dimensional Fourier Synthesis of Human Deoxyhaemoglobin at 3.5 Å Resolution , 1970, Nature.

[110]  Q. Gibson,et al.  Organic phosphates and the reaction of N-butyl isocyanide with human hemoglobin. , 1970, Biochemical and biophysical research communications.

[111]  R. Huber,et al.  Structures of deoxy- and carbonmonoxy-erythrocruorin. , 1970, Journal of molecular biology.

[112]  R. Shulman,et al.  Proton NMR studies of hemoglobin in H2O. , 1970, Biochemical and biophysical research communications.

[113]  S. Edelstein,et al.  Functional aspects of the subunit association-dissociation equilibria of hemoglobin. , 1970, The Journal of biological chemistry.

[114]  H. Gutfreund,et al.  Reactions of Haemoglobin Dimers after Ligand Dissociation , 1970, Nature.

[115]  Q. Gibson.  The reaction of oxygen with hemoglobin and the kinetic basis of the effect of salt on binding of oxygen. , 1970, Journal of Biological Chemistry.

[116]  R. Gray.  The kinetics of the alkaline Bohr effect of human hemoglobin. , 1970, Journal of Biological Chemistry.

[117]  H. Bunn,et al.  The interaction of 2,3-diphosphoglycerate with various human hemoglobins. , 1970, The Journal of clinical investigation.

[118]  M. Brunori,et al.  Artificial intermediates in the reaction of haemoglobin. Functional and conformational properties of the cyanmet intermediates. , 1970, Journal of molecular biology.

[119]  H. Bunn,et al.  Some observations on the properties of hemoglobin M Milwaukee-1. , 1970, Journal of molecular biology.

[120]  D. G. Davis,et al.  Nuclear magnetic resonance studies of hemoglobin. IV. The structure-function relationship of human adult hemoglobins A and Chesapeake and its implication to the nature of oxygenation of hemoglobin. , 1970, Biochemical and biophysical research communications.

[121]  R. Briehl,et al.  Ultraviolet difference spectra in human hemoglobin. I. Difference spectra in hemoglobin A and their relation to the function of hemoglobin. , 1970, The Journal of biological chemistry.

[122]  D. Irvine,et al.  Reactivity differences between haemoglobins. Ppart XVII. The variability of the Bohr effect between species and the effect of 2,3-diphosphoglyceric acid on the Bohr effect , 1970 .

[123]  O. W. van Assendelft,et al.  Spectrophotometry of haemoglobin derivatives , 1970 .

[124]  G. Stamatoyannopoulos,et al.  Single Chain Alkali Resistance in Hemoglobin Rainier: β 145 Tyrosine → Histidine , 1969, Science.

[125]  J. Haber,et al.  Evidence for β-β interactions during the binding of oxygen to hemoglobin , 1969 .

[126]  H. Morimoto,et al.  Properties of hemoglobin M, Milwaukee-I variant and its unique characteristic. , 1969, Biochimica et biophysica acta.

[127]  Q. Gibson,et al.  Preparation and Properties of α- and β-Chains from Human Hemoglobin , 1969 .

[128]  D. Collins,et al.  Stereochemistry of the low-spin iron porphyrin, bis(imidazole)-alpha,beta,gamma,delta-tetraphenylporphinatoiron (3) chloride. , 1969, Journal of the American Chemical Society.

[129]  M. Brunori,et al.  Kinetic studies of ligand binding to hemoglobin and its isolated subunits by the temperature jump relaxation method. , 1969, The Journal of biological chemistry.

[130]  M. Brunori,et al.  On the rate of a conformation change associated with ligand binding in hemoglobin. , 1969, The Journal of biological chemistry.

[131]  M. Brunori,et al.  Oxidation-reduction equilibrium of human hemoglobin in concentrated sodium chloride solutions. Consistency with the (alpha beta) dimer model. , 1969, Biochemistry.

[132]  L. Rossi-Bernardi,et al.  Inhibition of CO2 Combination and Reduction of the Bohr Effect in Haemoglobin chemically modified at its α-Amino Groups , 1969, Nature.

[133]  L. Mazzarella,et al.  Identification of Residues responsible for the Alkaline Bohr Effect in Haemoglobin , 1969, Nature.

[134]  R. Cassoly,et al.  Preparation and properties of the isolated α and β chains of human hemoglobin in the ferri state: Investigation of oxidation-reduction equilibria , 1969 .

[135]  R. Cassoly,et al.  Oxygen equilibria of human hemoglobin valency hybrids. Discussion on the intrinsic properties of alpha and beta chains in the native protein. , 1969, Journal of molecular biology.

[136]  R. Benesch,et al.  The oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration. , 1969, Biochemistry.

[137]  H. Mcconnell,et al.  Spin-labeled hemoglobin derivatives in solution, polycrystalline suspensions, and single crystals. , 1969, Biochemistry.

[138]  R. Benesch,et al.  Intracellular Organic Phosphates as Regulators of Oxygen Release by Haemoglobin , 1969, Nature.

[139]  R. Noble.  Relation between allosteric effects and changes in the energy of bonding between molecular subunits. , 1969, Journal of molecular biology.

[140]  Q. Gibson,et al.  Kinetic evidence for a tetrameric functional unit in hemoglobin. , 1968, The Journal of biological chemistry.

[141]  M. Perutz,et al.  Molecular Pathology of Human Haemoglobin , 1968, Nature.

[142]  H. Muirhead,et al.  Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution : (I) X-ray Analysis , 1968, Nature.

[143]  M. Perutz,et al.  Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model , 1968, Nature.

[144]  M. Brunori,et al.  Spectral differences between haemoglobin and isolated haemoglobin chains in the deoxygenated state , 1968 .

[145]  M. Brunori,et al.  Studies on the oxidation-reduction potentials of heme proteins. VII. Oxidation-reduction equilibrium of hemoglobin bound to haptoglobin. , 1968, The Journal of biological chemistry.

[146]  R. Nagel,et al.  Oxygen equilibrium of hemoglobin M-Hyde Park. , 1968, Biochimica et biophysica acta.

[147]  R. Jones,et al.  Erythrocytosis secondary to increased oxygen affinity of a mutant hemoglobin, hemoglobin Kempsey. , 1968, Blood.

[148]  J. Bonaventura,et al.  Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and an abnormal oxygen equilibrium. , 1968, The Journal of biological chemistry.

[149]  K. Imai.  Oxygen-equilibrium characteristics of abnormal hemoglobin Hiroshima (α2β2143 Asp) , 1968 .

[150]  J. Wyman,et al.  Properties of the alpha and beta chains of hemoglobin prepared from their mercuribenzoate derivatives by treatment with 1-dodecanethiol. , 1967, The Journal of biological chemistry.

[151]  M. Novy,et al.  Hemoglobin Yakina. II. High blood oxygen affinity associated with compensatory erythrocytosis and normal hemodynamics. , 1967, The Journal of clinical investigation.

[152]  Richard T. Jones,et al.  Hemoglobin Yakima: I. Clinical and Biochemical Studies , 1967 .

[153]  M. Brunori,et al.  Observations on the kinetics of the reaction of hemoglobin with oxygen. , 1967, The Journal of biological chemistry.

[154]  H. Morimoto,et al.  Changes in EPR spectra of M-type abnormal haemoglobins induced by deoxygenation and their implications for the haem-haem interaction. , 1967, Biochimica et biophysica acta.

[155]  L. Mazzarella,et al.  Structure and function of haemoglobin: IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 Å resolution , 1967 .

[156]  A. Chanutin,et al.  Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocytes. , 1967, Archives of biochemistry and biophysics.

[157]  R. Hill,et al.  The pK of Specific Groups of Proteins I. THE α-AMINO GROUP OF THE α CHAIN OF HUMAN CO-HEMOGLOBIN , 1967 .

[158]  E. Huehns,et al.  On the mechanism of the dissociation of haemoglobin. , 1967, Journal of molecular biology.

[159]  R. Benesch,et al.  The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. , 1967, Biochemical and biophysical research communications.

[160]  M. Perutz,et al.  Identity of structure of horse deoxy- and oxyhaemoglobin after reaction with bis(N-maleidomethyl)ether. , 1967, Journal of molecular biology.

[161]  M. Brunori,et al.  The reactions of the isolated alpha and beta chains of human hemoglobin with oxygen and carbon monoxide. , 1966, The Journal of biological chemistry.

[162]  H. Lehmann,et al.  Hemoglobin J Cape Town-alpha-2 92 arginine replaced by glutamine beta-2. , 1966, Nature.

[163]  J P Changeux,et al.  On the nature of allosteric transitions: implications of non-exclusive ligand binding. , 1966, Journal of molecular biology.

[164]  A. Hayashi,et al.  The oxygen equilibrium of hemoglobin MSaskatoon. , 1966, Biochimica et biophysica acta.

[165]  R. Benesch,et al.  The preparation and properties of the isolated alpha and beta subunits of hemoglobin A. , 1966, Biochemistry.

[166]  J. Clegg,et al.  Abnormal human haemoglobins , 1966 .

[167]  C. Tanford,et al.  Titration of the Histidyl and α-Amino Groups of Hemoglobin , 1966 .

[168]  J. Kendrew,et al.  Structure of Deoxymyoglobin : A Crystallographic Study , 1966, Nature.

[169]  N. Hayashi,et al.  Studies on relationships between structure and function of hemoglobin M-Iwate. , 1966, The Journal of biological chemistry.

[170]  D. Koshland,et al.  Comparison of experimental binding data and theoretical models in proteins containing subunits. , 1966, Biochemistry.

[171]  M. Brunori,et al.  STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. V. THE OXIDATION BOHR EFFECT IN NORMAL HUMAN HEMOGLOBIN AND HUMAN HEMOGLOBIN DIGESTED WITH CARBOXYPEPTIDASE A. , 1965, The Journal of biological chemistry.

[172]  A. Hayashi,et al.  Functional abnormality of hemoglobin M-Osaka. , 1965, Biochemical and biophysical research communications.

[173]  W. Caughey,et al.  The Crystal Structure and Molecular Stereochemistry of Methoxyiron (III) Mesoporphyrin-IX Dimethyl Ester1 , 1965 .

[174]  J. Wyman,et al.  THE PROPERTIES AND INTERACTIONS OF THE ISOLATED ALPHA AND BETA CHAINS OF HUMAN HAEMOGLOBIN. 3. OBSERVATIONS ON THE EQUILIBRIA AND KINETICS OF THE REACTIONS WITH GASES. , 1965, Journal of molecular biology.

[175]  J. Wyman,et al.  THE PROPERTIES AND INTERACTIONS OF THE ISOLATER ALPHA AND BETA CHAINS OF HUMAN HAEMOGLOBIN. I. SEDIMENTATION AND ELECTROPHORETIC BEHAVIOUR. , 1965, Journal of molecular biology.

[176]  J. Changeux,et al.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.

[177]  R. Nagel,et al.  OXYGEN EQUILIBRIA OF THE HEMOGLOBIN-HAPTOGLOBIN COMPLEX. , 1965, Biochimica et biophysica acta.

[178]  D. F. Koenig.  The structure of a-chlorohemin , 1965 .

[179]  A. Tsugita,et al.  THE STRUCTURAL STUDY ON A NEW HEMOGLOBIN VARIANT, HB MOSAKA. , 1965, Biochimica et biophysica acta.

[180]  M. Brunori,et al.  STUDIES ON THE RELATIONS BETWEEN MOLECULAR AND FUNCTIONAL PROPERTIES OF HEMOGLOBIN. V. THE INFLUENCE OF TEMPERATURE ON THE BOHR EFFECT IN HUMAN AND IN HORSE HEMOGLOBIN. , 1965, The Journal of biological chemistry.

[181]  J. Wyman,et al.  THE BINDING POTENTIAL, A NEGLECTED LINKAGE CONCEPT. , 1965, Journal of molecular biology.

[182]  M. O. Dayhoff,et al.  Atlas of protein sequence and structure , 1965 .

[183]  J. Wyman,et al.  THE EFFECT OF OXYGENATION ON THE RATE OF DIGESTION OF HUMAN HEMOGLOBINS BY CARBOXYPEPTIDASES. , 1964, The Journal of biological chemistry.

[184]  M. Brunori,et al.  STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. I. HUMAN HEMOGLOBIN. , 1964, The Journal of biological chemistry.

[185]  J. Wyman,et al.  LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. , 1964, Advances in protein chemistry.

[186]  J. Kendrew,et al.  THE MODE OF ATTACHMENT OF THE AZIDE ION TO SPERM WHALE METMYOGLOBIN. , 1964, Journal of molecular biology.

[187]  M. Brunori,et al.  STUDIES ON THE RELATIONS BETWEEN MOLECULAR AND FUNCTIONAL PROPERTIES OF HEMOGLOBIN. IV. THE BOHR EFFECT IN HUMAN HEMOGLOBIN MEASURED BY PROTON BINDING. , 1963, The Journal of biological chemistry.

[188]  M. Perutz,et al.  Structure Of Hæemoglobin: A Three-Dimensional Fourier Synthesis of Reduced Human Haemoglobin at 5.5 Å Resolution , 1963, Nature.

[189]  J. Kendrew.  Myoglobin and the structure of proteins. , 1963, Science.

[190]  P. Heller,et al.  Hemoglobin M Kankakee, a new variant of hemoglobin M. , 1962, Blood.

[191]  R. Benesch.  The influence of oxygenation on the reactivity of the--SH groups of hemoglobin. , 1962, Biochemistry.

[192]  J. Wyman,et al.  Studies on the relations between molecular and functional properties of hemoglobin. , 1962, The Journal of biological chemistry.

[193]  A. Riggs.  The binding of N-ethylmaleimide by human hemoglobin and its effect upon the oxygen equilibrium. , 1961, The Journal of biological chemistry.

[194]  R. Dickerson,et al.  A Partial Determination by X-ray Methods, and its Correlation with Chemical Data , 1961, Nature.

[195]  R. Benesch,et al.  The Chemistry of the Bohr Effect I. THE REACTION OF N-ETHYL MALEIMIDE WITH THE OXYGEN-LINKED ACID GROUPS OF HEMOGLOBIN , 1961 .

[196]  Q. Gibson.  The photochemical formation of a quickly reacting form of haemoglobin. , 1959, The Biochemical journal.

[197]  J. Wyman,et al.  The problem of the heme interactions in hemoglobin and the basis of the bohr effect , 1951 .

[198]  J. Wyman,et al.  INTERRELATIONSHIPS IN THE REACTIONS OF HORSE HEMOGLOBIN , 1941 .

[199]  C. D. Coryell,et al.  Magnetic Studies of Ferrihemoglobin Reactions. II. Equilibria and Compounds with Azide Ion, Ammonia, and Ethanol1 , 1940 .

[200]  J. Wyman.  THE HEAT OF OXYGENATION OF HEMOGLOBIN , 1939 .

[201]  F. Haurowitz,et al.  Das Gleichgewicht zwischen Hämoglobin und Sauerstoff. , 1938 .

[202]  C. D. Coryell,et al.  The Magnetic Properties and Structure of Ferrihemoglobin (Methemoglobin) and Some of its Compounds , 1937 .

[203]  G. Adair.  THE HEMOGLOBIN SYSTEM VI. THE OXYGEN DISSOCIATION CURVE OF HEMOGLOBIN , 1925 .

[204]  L. Henderson.  THE EQUILIBRIUM BETWEEN OXYGEN AND CARBONIC ACID IN BLOOD , 1920 .

[205]  John R. Christiansen,et al.  The absorption and dissociation of carbon dioxide by human blood , 1914, The Journal of physiology.

[206]  Christian Bohr,et al.  Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensäurespannung des Blutes auf dessen Sauerstoffbindung übt1 , 1904 .