Biochemical and Clinical Aspects of Hemoglobin Abnormalities

Winslow Caughey

• Publisher: Academic Press
• Year: 2012
• Print ISBN: 9780121643508
• eBook ISBN: 9780323142748
• Topic: Medicine
• Subtopic: Hematology

Biochemical and Clinical Aspects of Hemoglobin Abnormalities contains the proceedings of a symposium held on the Pingree Park campus of Colorado State University on October 2-7, 1977. Contributors discuss the biochemical and clinical aspects of hemoglobin abnormalities and cover topics ranging from amino acid substitutions to sickle cell disease, glycosylated hemoglobins, cystamine inhibition of sickling, and gelation of sickle cell hemoglobin. This volume is organized into 52 chapters and begins with a discussion of the role of distal residues in structure, ligand binding, and oxidation of hemoglobins A, Zurich, and Sydney. It then turns to functional abnormalities of whole blood in sickle cell anemia, inhibition of sickle hemoglobin gelation by amino acids and peptides, and intermolecular interactions in crystals of human deoxy hemoglobins A, C, F, and S. The chapters that follow focus on glycosylation of human hemoglobin, the phase transitions of sickle-cell hemoglobin, conformational effects of the HbS mutation, and mechanisms for hemoglobin oxidation. The reader is also introduced to oxidation of oxyhemoglobin by reductants, the kinetics of oxygen binding to human red blood cells, and oxidation of human hemoglobin by copper. A chapter that assesses the effect of physiological parameters, such as pH, oxygen concentration, protein concentration, non-gelling hemoglobins, and the erythrocyte membrane, on the kinetics of polymerization of deoxyhemoglobin S concludes the book. This book is intended for biochemists and clinicians interested in knowing more about hemoglobin abnormalities.

Table of contents

• Front Cover
• Biochemical and Clinical Aspects of Hemoglobin Abnormalities
• Copyright Page
• Table of Contents
• LIST OF CONTRIBUTORS
• PREFACE
• CHAPTER 1. ROLE OF DISTAL RESIDUES IN STRUCTURE, LIGAND BINDING AND OXIDATION OF HEMOGLOBINS A, ZÜRICH, AND SYDNEY
• CHAPTER 2. PROPERTIES AND REACTION MECHANISM OF Hb ZÜRICH (α2β2HIS (63) → ARG)
• CHAPTER 3. LIGAND BINDING TO HEMOGLOBINS: EFFECTS OF GLOBIN STRUCTURE
• CHAPTER 4. FUNCTIONAL ABNORMALITIES OF WHOLE BLOOD IN SICKLE CELL ANEMIA
• CHAPTER 5. HEMOSTATIC ALTERATIONS IN SICKLE CELL ANEMIA
• CHAPTER 6. ASSESSMENT OF THE CLINICAL SEVERITY OF SICKLE CELL DISEASE
• CHAPTER 7. LOCATION OF THE HEME IRON ATOMS AND CHARACTERIZATION OF THE QUATERNARY STRUCTURE OF THE CARBONMONOXY-β4 TETRAMER
• CHAPTER 8. HEMOGLOBIN ENGINEERING: CONSEQUENCES OF ALTERATIONS AT FUNCTIONALLY SENSITIVE SITES PARTICULARLY SUSCEPTIBLE TO CHEMICAL OR ENZYMATIC ATTACK
• CHAPTER 9. THE OXYGEN BINDING IN ABNORMAL COBALT MYOGLOBINS AND HEMOGLOBINS"
• CHAPTER 10. AMINO ACIDS AND PEPTIDES AS INHIBITORS OF SICKLE HEMOGLOBIN GELATION
• CHAPTER 11. EFFECT OF DBA ON HEMOGLOBIN SS CELLS AND HEMOGLOBIN BIOSYNTHESIS
• CHAPTER 12. PROGRESS IN THE NATURAL HISTORY STUDIES OF THE CLINICAL SEVERITY OF SICKLE CELL DISEASE: EPIDEMIOLOGIE ASPECTS
• CHAPTER 13. INTERMOLECULAR INTERACTIONS IN CRYSTALS OF HUMAN DEOXY HEMOGLOBINS A, C, F, AND S
• CHAPTER 14. PROTON NUCLEAR MAGNETIC RESONANCE STUDIES OF SICKLE CELL HEMOGLOBIN
• CHAPTER 15. AREAS OF INTERACTION IN THE HbS POLYMER
• CHAPTER 16. GLYCOSYLATED HEMOGLOBINS
• CHAPTER 17. GLYCOSYLATION OF HUMAN HEMOGLOBIN
• CHAPTER 18. EVALUATION OF THE POOL OF α HEMOGLOBIN CHAINS AND STUDY OF THE DISSOCIATION OF THE HEMOGLOBIN MOLECULE INTO MONOMERS
• CHAPTER 19. INHIBITION OF SICKLING BY CYSTAMINE
• CHAPTER 20. PROGRESS IN INTERPRETING THE PHASE TRANSITIONS OF SICKLE-CELL HEMOGLOBIN
• CHAPTER 21. CIRCULAR DICHROISM PROBES OF HEMOGLOBIN STRUCTURE
• CHAPTER 22. CONFORMATIONAL EFFECTS OF THE HbS MUTATION
• CHAPTER 23. ELECTRON MICROSCOPY OF FIBERS AND CRYSTALS OF A DEOXYGENATED PLATINUM DERIVATIVE OF HEMOGLOBIN S
• CHAPTER 24. OPTICAL DETECTION OF HEME LIGAND CONFIGURATION IN SPERM WHALE MYOGLOBIN
• CHAPTER 25. THE ROLE OF SPECTRIN AND ACTIN IN IRREVERSIBLY SICKLED CELLS: UNSICKLING OF "IRREVERSIBLY" SICKLED GHOSTS BY CONDITIONS WHICH INTERFERE WITH SPECTRIN-ACTIN POLYMERIZATION
• CHAPTER 26. SPECTRIN ASSEMBLY IN IRREVERSIBLY SICKLED CELL MEMBRANES: ROLE OF CALCIUM AND ATP
• CHAPTER 27. HEMOGLOBIN INTERACTIONS AND WHOLE BLOOD OXYGEN EQUILIBRIUM CURVES IN SICKLING DISORDERS
• CHAPTER 28. DETERMINATION OF THE STRUCTURE OF THE FIBERS OF HEMOGLOBIN S BY ELECTRON MICROSCOPY AND THREE-DIMENSIONAL IMAGE RECONSTRUCTION
• CHAPTER 29. FUNCTIONAL IDENTITY OF HEMOGLOBINS S AND A IN THE ABSENCE OF POLYMERIZATION
• CHAPTER 30. THE APPARENT ABSENCE OF A LIGAND-LINKED STRUCTURAL TRANSITION IN THE REGION OF THE ß6 VALINE OF HEMOGLOBIN S
• CHAPTER 31. LIGAND BINDING AND THE GELATION OF SICKLE CELL HEMOGLOBIN
• CHAPTER 32. SUCCESSES AND FAILURES OF A SIMPLE NUCLEATION THEORYFOR SICKLE CELL HEMOGLOBIN GELATION
• CHAPTER 33. REDOX SYSTEM: IRON (II) -IRON (III) INTERCONVERSION IN OXYGEN-CARRYING PROTEINS
• CHAPTER 34. MECHANISMS FOR HEMOGLOBIN OXIDATION: THE RESPONSE OF ABNORMAL HUMAN AND OTHER HEMOGLOBINS TO DIFFERENT OXIDATIVE PATHWAYS
• CHAPTER 35. OXIDATION OF OXYHEMOGLOBIN BY REDUCTANTS
• CHAPTER 36. CROSSINGS OVER VERSUS POINT MUTATIONS AS CAUSES OF HEMOGLOBIN VARIANTS AND POSSIBLY OF THALASSEMIAS
• CHAPTER 37. HEMOGLOBIN AND THE RED CELL MEMBRANE
• CHAPTER 38. STRUCTURAL ASPECTS OF HEMOGLOBIN FUNCTION
• CHAPTER 39. EFFECTS OF HEME IRON LIGANDS ON SELF-ASSOCIATION OF ßSH CHAINS
• CHAPTER 40. ALLOSTERIC BINDING HEAT EFFECTS OF HbA AND HbM IWATE
• CHAPTER 41. ANALYSIS OF OXYGEN EQUILIBRIA IN SYNTHETIC AND NATURAL MUTANT VALENCE HYBRID HEMOGLOBINS: IMPLICATIONS FOR MODELS OF HEME-HEME INTERACTION IN NORMAL HEMOGLOBIN
• CHAPTER 42. THE KINETICS OF OXYGEN BINDING TO HUMAN RED BLOOD CELLS
• CHAPTER 43. MEASUREMENT OF HOMEOSTATIC RESPONSES TO ALTERED P50 IN PATIENTS WITH ABNORMAL HEMOGLOBINS
• CHAPTER 44. OXIDATION OF HUMAN HEMOGLOBIN BY COPPER: SPECIFICITY FOR BETA CHAINS AND FORMATION OF MODIFIED PRECURSOR
• CHAPTER 45. DICHLOROMETHANE AS AN ANTISICKLING AGENT IN SICKLE CELL HEMOGLOBIN
• CHAPTER 46. FOURIER TRANSFORM INFRARED SPECTROSCOPY OF HEMOGLOBIN
• CHAPTER 47. A COMPARATIVE EPR STUDY OF HEMOGLOBINS A AND KANSAS: SPECTRAL SIGNATURES OF AFFINITY STATES
• CHAPTER 48. IONIC AND NON-IONIC EFFECTS ON THE SOLUBILITY OF DEOXYHEMOGLOBIN S
• CHAPTER 49. ANIONIC CONTROL OF HEMOGLOBIN FUNCTION
• CHAPTER 50. INHIBITION OF ERYTHROCYTE SICKLING IN VITRO BY GLYCERALDEHYDE
• CHAPTER 51. MAJOR SITES FOR THE OXYGEN-LINKED BINDING OF CHLORIDE TO HEMOGLOBIN
• CHAPTER 52. EFFECTORS OF THE RATE OF DEOXYHEMOGLOBIN S POLYMERIZATION
• INDEX