Gelation of sickle cell haemoglobin. II. Methaemoglobin.
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[1] C. D. de Verdier,et al. Binding of 2,3-diphosphoglycerate and adenosine triphosphate to human haemoglobin A. , 2005, European journal of biochemistry.
[2] 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.
[3] A. Fersht,et al. Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin. , 1974, Biochemistry.
[4] M. Perutz,et al. Structure of inositol hexaphosphate–human deoxyhaemoglobin complex , 1974, Nature.
[5] M. R. Mauk,et al. Activation of methaemoglobin peroxidase by inositol hexaphosphate. , 1973, Nature: New biology.
[6] R. Briehl,et al. Effects of pH, 2,3-diphosphoglycerate and salts on gelation of sickle cell deoxyhemoglobin. , 1973, Journal of molecular biology.
[7] L Anderson,et al. Intermediate structure of normal human haemoglobin: methaemoglobin in the deoxy quaternary conformation. , 1973, Journal of molecular biology.
[8] J. Kilmartin. The interaction of inositol hexaphosphate with methaemoglobin. , 1973, The Biochemical journal.
[9] K. Ruckpaul,et al. Magneto‐optical rotation spectra of methemoglobin in the presence of allosteric effectors , 1973, FEBS letters.
[10] M. F. Perutz,et al. Nature of Haem–Haem Interaction , 1972, Nature.
[11] A. Arnone. X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin , 1972, Nature.
[12] L. Gilbert,et al. Dissociation of oxyhaemoglobin, methaemoglobin and their hybrid compared by difference gel chromatography. , 1972, Nature: New biology.
[13] O. Ristau,et al. On the influence of ATP on the electron paramagnetic resonance spectrum of methemoglobin , 1971, FEBS letters.
[14] O. Ristau,et al. Interaction of hemoglobin with ions. Allosteric effects of the binding of anions. , 1971, Biochimica et biophysica acta.
[15] M. Perutz. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery , 1970, Nature.
[16] S. Ohnishi,et al. A kinetic study on conformational change of deoxyhemoglobin induced by a group of effectors. , 1970, Biochemical and biophysical research communications.
[17] 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.
[18] T. Hollocher,et al. Electron spin resonance studies of native and denatured methemoglobin. pH effects. , 1966, The Journal of biological chemistry.
[19] J. Changeux,et al. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.
[20] B. Ames,et al. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. , 1960, The Journal of biological chemistry.
[21] C. D. Coryell,et al. The Magnetic Properties and Structure of Ferrihemoglobin (Methemoglobin) and Some of its Compounds , 1937 .
[22] M. Perutz. Methaemoglobin and the Problem of Haem-Haem Interaction , 1973 .
[23] M. Rörth,et al. An enzymatic assay of 2,3-diphosphoglycerate in blood. , 1969, Scandinavian journal of clinical and laboratory investigation.