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.
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