Hemoglobin and Red Cell Structure and Function

1. Front Matter

   Pages i-xxxii

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2. Hemoglobin Structure and Function

   1. Front Matter

      Pages 1-1

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   2. Structure of Haemoglobin M Milwaukee, A Mutant Form Exhibiting Interaction Between Ferrous and Ferric Subunits

      • M. F. Perutz, P. D. Pulsinelli, Helen M. Ranney

      Pages 3-18

   3. The Interaction Between Hemoglobin and Its “Oxygen-Linked” Ligands

      • O. Brenna, M. Luzzana, M. Pace, M. Perrella, F. Rossi, L. Rossi-Bernardi et al.

      Pages 19-40

   4. The Interaction of Sickle Hemoglobin with DPG, CO2 and with Other Hemoglobins: Formation of Asymmetrical Hybrids

      • H. Franklin Bunn

      Pages 41-53

   5. Enhancement of the Acid and Alkaline Bohr Effects of Hemoglobin by Organic Phosphates

      • Austen Riggs, Takashi Imamura

      Pages 55-63

   6. Functional Non-Equivalence of α and β Hemes in Human Hemoglobins

      • Chien Ho, Ted R. Lindstrom

      Pages 65-76

3. Red Cell Metabolism and Function

   1. Front Matter

      Pages 77-77

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   2. Hemoglobin Casper G8 β106 Leu→ Pro: Further Evidence that Hemoglobin Mutations are Not Random

      • R. T. Jones, R. D. Koler, M. Duerst, Z. Stocklen

      Pages 79-98

   3. Potential Effects of Hemoglobin Concentration on Red Cell Metabolism Together with Observations on Red Cell Metabolic Differences Between Men and Women

      • George J. Brewer, Fred J. Oelshlegel Jr., Eric B. Schoomaker, Conrad A. Knutsen

      Pages 99-119

   4. Catalase Activity and Red Cell Metabolism

      • John W. Eaton, Martin Boraas, Nina L. Etkin

      Pages 121-131

   5. Red Cell Hexosemonophosphate Shunt Deficiency in Uremia

      • Harry Jacob, Yoshihito Yawata, Robert Howe

      Pages 133-143

   6. Effect of Inorganic Phosphate on Red Cell Metabolism: In Vitro and In Vivo Studies

      • Michael C. Brain, Robert T. Card

      Pages 145-154

   7. Studies of the Metabolic Basis of the ATP-DPG Differences in Genetically Selected High and Low ATP-DPG Rat Strains

      • Nancy A. Noble, George J. Brewer

      Pages 155-164

4. Carbonic Anhydrase and Carbon Dioxide Transport

   1. Front Matter

      Pages 165-165

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   2. Introductory Remarks at the Beginning of Session III

      • Richard E. Tashian

      Pages 167-168

   3. Functional Aspects of the Three-Dimensional Structure of the Active Site of Carbonic Anhydrase

      • Ivar Waara, Seved Lövgren, Anders Liljas, K. K. Kannan, Per-Christer Bergstén

      Pages 169-187

   4. The Effect of Temperature on the Catalytic Activity of Bovine Carbonic Anhydrase

      • John C. Kernohan

      Pages 189-199

   5. Carbonic Anhydrase, Red Cell Membranes, and CO2 Transport

      • Theodore Enns

      Pages 201-208

   6. Effect of Chlorthalidone Binding on the Electrophoretic Properties of Human Red Cell Carbonic Anhydrase Isozymes

      • Richard E. Tashian, Ya-Shiou L. Yu

      Pages 209-213

Hemoglobin and the red cell have continued to set a dizzying pace as the objects of research in the two and one-half year interval since the First International Conference on Red Cell Metabolism and Function. Most exciting perhaps, is a beginning molecular attack on sickle cell disease. The story of the inter­ action of red cell metabolism and oxygen transport has continued to unfold, and we can now infer that patients with hypoxia usually utilize red cell metabolic adjustments to improve oxygenation. This puts the red cell squarely in the center of medical practice, since much of medicine-heart, pulmonary, and blood disease- deals with inadequate oxygenation. On April 27th through the 29th, 1972, crystallographers, chemists, biochemists, physiologists, geneticists, and physi­ cians from many medical disciplines met in the Towsley Center for Continuing Medical Education at the University of Michigan, Ann Arbor to present new data, to review recent developments, and to try to piece together additional features of the red cell puzzle. The meeting was dedicated to Dr. Francis John Worsley Roughton, Professor Emeritus of Colloid Science, University of Cambridge, England, in recognition of his numerous excellent contributions to the understanding of hemoglobin and red cell function. The program got off to a good start with a paper from M. F. Perutz, Nobel Laureate, on the structure of hemoglobin. Dr.

• anemia
• blood
• cell
• cognition
• development
• education
• hypoxia
• medical education
• medical practice
• medicine
• metabolism
• patients
• research
• transport

• Department of Human Genetics and Medicine (Simpson Memorial Institute), University of Michigan, Ann Arbor, USA

  George J. Brewer

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