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Abstract

The conspicuous red color of the blood has no doubt been a source of wonder, interest, and curiosity ever since it was first observed by man. It followed much later that hemoglobin, the cause of the red color, is neatly packaged in the red blood cells apart from the other constituents of the blood and that it serves as a carrier for oxygen in the body. Not only the oxygen-carrying function of hemoglobin has been the subject of much research but almost every chemical or physiological topic related to hemoglobin has received attention until, at the present time, the literature on hemoglobin is almost overwhelming in amount. No small part of this vast literature has come during the last ten years, since the discovery by Pauling, Itano, Singer, and Wells (99) of the first abnormal human hemoglobin which is now termed sickle-cell anemia hemoglobin or hemoglobin S. This discovery gave a new impetus to the study of hematological disorders for here, for the first time, was a pathological state unquestionably associated with a molecule that is slightly different in some way from the normal one. Because of this difference it is unable to function properly: a molecular disease had been detected. The detection of other abnormal hemoglobins soon followed so that today almost all the letters of the alphabet have been used to designate the various abnormal hemoglobins.

It is a pleasure to acknowledge that during the preparation of this article the author had many stimulating discussions with Dr. Richard T. Jones, Dr. Jerome Vinograd, and Dr. Norman Weliky, and that some of the ideas expressed here arose from these discussions.

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References

  1. Adair, G. S.: A Comparison of the Molecular Weights of the Proteins. Proc. Cambridge Phil. Soc. 1, 75 (1924).

    CAS  Google Scholar 

  2. Akabori, S., K. Ohno, T. Ikenaka, Y. Okada, H. Hanafusa, I. Haruna, A. Tsugita, K. Sugae and T. Matsushima: Hydrazinolysis of Peptides and Proteins. II. Fundamental Studies on the Determination of the Carboxyl Ends of Proteins. Bull. Chem. Soc. Japan 29, 507 (1956).

    Article  CAS  Google Scholar 

  3. Allen, D. W., K. F. Guthe and J. Wyman, Jr.: Further Studies on the Oxygen Equilibrium of Hemoglobin. J. Biol. Chem. 187, 393 (1950).

    CAS  Google Scholar 

  4. Allen, D. W. and W. A. Schroeder: A Comparison of the Phenylalanine Content of the Hemoglobin of Normal and Phenylketonuric Individuals: Determination by Ion Exchange Chromatography. J. Clin. Investigation 36, 1343 (1957)

    Article  CAS  Google Scholar 

  5. Allen, D. W., W. A. Schroeder and J. Balog: Observations on the Chromatographic Heterogeneity of Normal Adult and Fetal Human Hemoglobin: A Study of the Effects of Crystallization and Chromatography on the Heterogeneity and Isoleucine Content. J. Amer. Chem. Soc. 80, 1628 (1958).

    Article  CAS  Google Scholar 

  6. Allison, A. C.: Notation for Hemoglobin Types and Genes Controlling Their Synthesis. Science (Washington) 122, 640 (1955).

    Article  CAS  Google Scholar 

  7. Allison, A. C. and R. Cecil: The Thiol Groups of Normal Adult Human Haemoglobin. Biochemic. J. 69, 27 (1958).

    CAS  Google Scholar 

  8. Anonymous: Statement Concerning a System of Nomenclature for the Varieties of Human Hemoglobin. Blood 8, 386 (1953).

    Google Scholar 

  9. Anson, M. L. and A. E. Mirsky: Protein Coagulation and its Reversal. The Preparation of Insoluble Globin, Soluble Globin, and Heme. J. Gen. Physiol. 13, 469 (1929/30).

    Google Scholar 

  10. Bangham, A. D. and H. Lehmann: “Multiple” Haemoglobins in the Horse. Nature (London) 181, 267 (1958).

    Article  CAS  Google Scholar 

  11. Barrett, H. W. and W. A. Schroeder: unpublished.

    Google Scholar 

  12. Beaven, G. H., H. Hoch and E. R. Holiday: The Haemoglobins of the Human Foetus and Infant. Electrophoretic and Spectroscopic Differentiation of Adult and Foetal Types. Biochemic. J. 49, 374 (1951).

    CAS  Google Scholar 

  13. Benesch, R. E., H. A. Lardy and R. Benesch: The Sulfhydryl Groups of Crystalline Proteins. I. Some Albumins, Enzymes, and Hemoglobins. J. Biol. Chem. 216, 663 (1955)

    CAS  Google Scholar 

  14. Bernhart, F. W. and L. Skeggs: The Iron Content of Crystalline Human Hemoglobin. J. Biol. Chem. 147, 19 (1943).

    CAS  Google Scholar 

  15. Betke, K.: Der menschUche rote Blutfarbstoff bei Fetus und reifem Organismus. Berlin: Springer-Verlag. 1954

    Google Scholar 

  16. Bragg, W. L. and M. F. Perutz: The External Form of the Hemoglobin Molecule. II. Acta Crystallogr. 5, 323 (1952).

    Article  CAS  Google Scholar 

  17. Brown, H.: The Free Amino Groups and Terminal Dipeptides of Human Adult Hemoglobin. Arch. Biochem. Biophys. 61, 241 (1956).

    Article  CAS  Google Scholar 

  18. The Sulfur Distribution and Some Cysteic Acid Peptides of Human Adult Hemoglobin. Arch. Biochem. Biophys. 67, 256 (1957).

    Google Scholar 

  19. Cabannes, R. et CH. Serain: Étude électrophorétique des hémoglobines des Mammifères domestiques d’Algérie. C. R. Séances Soc. Biol. 149, 1193 (1955)

    Google Scholar 

  20. Chernoff, A. I.: The Alkali Denaturation Procedures. In: Conference on Hemoglobin. Nat. Acad. Sci., National Research Council, Washington, D. C., Publication No. 557, 1958, p. 172.

    Google Scholar 

  21. Immunologie Aspects of the Human Hemoglobin. In: Conference on Hemoglobin. Nat. Acad. Sci., National Research Council, Washington, D. C., Publication No. 557, 1958, p. 179.

    Google Scholar 

  22. Clegg, M. and W. A. Schroeder: J. Amer. Chem. Soc. (1959)

    Google Scholar 

  23. Cole, R. D., W. H. Stein and S. Moore: On the Cysteine Content of Human Hemoglobin. J. Biol. Chem. 233, 1359 (1958).

    CAS  Google Scholar 

  24. Conference on Hemoglobin. Nat. Acad. Sci., National Research Council, Washington, D. C., Publication No. 557, 1958.

    Google Scholar 

  25. Cook, J. L. and M. Morrison: Ion Exchange Chromatography of Human Hemoglobin. Federat. Proc. (Amer. Soc. exp. Biol.) 15, 235 (1956).

    Google Scholar 

  26. Coryell, C. D. and L. Pauling: A Structural Interpretation of the Acidity of Groups Associated with the Hemes of Hemoglobin and Hemoglobin Derivatives. J. Biol. Chem. 132, 769 (1940)

    CAS  Google Scholar 

  27. Craig, L. C., T. P. King and A. Stracher: Dialysis Studies. II. Some Experiments Dealing with the Problem of Selectivity. J. Amer. Chem. Soc. 79, 3729 (1957)

    Article  CAS  Google Scholar 

  28. Craig, L. C., W. Königsberg, A. Stracher and T. P. King: The Characterization of Lower Molecular Weight Proteins by Dialysis. In: A. Neuberger, Symposium on Protein Structure, p. 104. New York: Wiley and Sons. 1958.

    Google Scholar 

  29. Cullis, A. F., H. M. Dintzis and M. F. Perutz: X-Ray Analysis of Haemoglobin. In: Conference on Hemoglobin. Nat. Acad. Sei., National Research Council, Washington, D. C., Publication No. 557, 1958, p. 50.

    Google Scholar 

  30. Derrien, Y.: Studies on the Heterogeneity of Adult and Fetal Hemoglobins by Salting-out, Alkali Denaturation and Moving Boundary Electrophoresis. In: Conference on Hemoglobin. Nat. Acad. Sei., National Research Council, Washington, D. C., Publication No. 557, 1958, p. 183.

    Google Scholar 

  31. Dickman, S. R. and I. H. Moncrief: Primary Amide Groups of Human Hemoglobin. Proc. Soc. exp. Biol. Med. 77, 631 (1951).

    CAS  Google Scholar 

  32. Drabkin, D. L.: Metabolism of the Hemin Chromoproteins. Physiol. Rev. 31, 345 (1951).

    CAS  Google Scholar 

  33. Drabkin, D. L.: Symposium on Molecular Heterogeneity of Hemoglobin. Federat. Proc. (Amer. Soc. exp. Biol.) 16, 740–773 (1957)

    CAS  Google Scholar 

  34. Heredity and Environment in Structure of Hemoglobin. Federat. Proc. (Amer. Soc. exp. Biol.) 16, 740 (1957).

    Google Scholar 

  35. Drescher, H. und W. Künzer: Der Blutfarbstoff der menschlichen Feten. Klin. Wschr. 32, 92 (1954).

    Google Scholar 

  36. Dustin, J. P., G. Schapira, J. C. Dreyfus et O. Hestermans-Medard: La composition en acides aminés de l’hémoglobine foetale humaine. C. R. Séances Soc. Biol. 148, 1207 (1954).

    CAS  Google Scholar 

  37. Eastman, N. J.: Obstetrics. loth ed., p. 168. New York: Appleton-Century- Crofts. 1950.

    Google Scholar 

  38. Ferry, R. M. and A. A. Green: Studies in the Chemistry of Hemoglobin. III. The Equilibrium between Oxygen and Hemoglobin and its Relation to Changing Hydrogen Ion Activity. J. Biol. Chem. 81, 175 (1929)

    CAS  Google Scholar 

  39. Field, E. O. and J. R. P. O’Brien: Dissociation of Human Haemoglobin at Low pH. Biochemic. J. 60, 656 (1955).

    CAS  Google Scholar 

  40. George, P. and R. L. J. Lyster: A Survey of the Evidence for and against a Crevice Configuration for the Heme in Hemoglobin. In: Conference on Hemoglobin. Nat. Acad. Sei., National Research Council, Washington, D. C., Publication No. 557, 1958, p. 33.

    Google Scholar 

  41. Gutter, F. J., H. A. Sober and E. A. Peterson: The Effect of Mercaptoethanol and Urea on the Molecular Weight of Hemoglobin. Arch. Biochem. Biophys. 62, 427 (1956).

    Article  CAS  Google Scholar 

  42. Halbrecht, I. and C. Klibanski: Identification of a New Normal Embryonic Haemoglobin. Nature (London) 178, 794 (1956).

    Article  CAS  Google Scholar 

  43. Halbrecht, I., C. Klibanski, H. Brzoza and M. Lahav: Hemoglobins and the Serum Protein Fractions in Early Embryonic Life. Amer. J. Clin. Pathol. 29, 340 (1958) [Chem. Abstr. 52, 130, 61 (1958)].

    Google Scholar 

  44. Hasserodt, U. and M. Clegg: unpublished.

    Google Scholar 

  45. Hasserodt, U. and J. Vinograd: Dissociation of Human Carbonmonoxy- hemoglobin at High pH. Proc. Nat. Acad. Sei. (USA) 45, 12 (1959)

    Article  CAS  Google Scholar 

  46. Hasserodt, U., J. Vinograd and R. Srinivasan: The Molecular Weight of Human Hemoglobin. J. Amer. Chem. Soc. (in press).

    Google Scholar 

  47. Haurowitz, F. and R. L. Hardin: Respiratory Proteins. In: H. Neurath and K. Bailey, The Proteins, Vol. II A, p. 328. New York: Academic Press. 1954.

    Google Scholar 

  48. Havinga, E.: Comparison of the Phosphorus Content, Optical Rotation, Separation of Hemes and Globin, and Terminal Amino Acid Residues of Normal Adult Human Hemoglobin and Sickle Cell Anemia Hemoglobin. Proc. Nat. Acad. Sci. (USA) 39, 59 (1953).

    Article  CAS  Google Scholar 

  49. Hommes, F. A., A. Dozy and T. H. J. Huisman: Further Studies on the Cysteine-Cystine Content of the Foetal Human Haemoglobin. Biochemic. J. 68, 309 (1958)

    CAS  Google Scholar 

  50. Hommes, F. A., J. Santema-Drinkwaard and T. H. J. Huisman: The Sulfhydryl Groups of Four Different Human Haemoglobins. Biochim. Biophys. Acta 20, 564 (1956).

    Article  CAS  Google Scholar 

  51. Huisman, T. H. J.: The Properties, Estimation Methods, Hematologic Features, and Some Other More General Aspects of Different Abnormal Human Hemoglobins. Clin. Chem. 3, 371 (1957)

    CAS  Google Scholar 

  52. Huisman, T. H. J.: Abnormal Hemoglobins. Chn. Chim. Acta 3, 201 (1958).

    Article  CAS  Google Scholar 

  53. Huisman, T. H. J. and A. Dozy: The Action of Carboxypeptidase on Different Human Haemoglobins. Biochim. Biophys. Acta 20, 400 (1956).

    Article  CAS  Google Scholar 

  54. Huisman, T. H. J. and J. Drinkwaard: The N-terminal Residues of Five Different Human Haemoglobins. Biochim. Biophys. Acta 18, 588 (1955).

    Article  CAS  Google Scholar 

  55. Huisman, T. H. J., J. H. P. Jonxis and A. Dozy: Is Foetal Haemoglobin Present in the Blood of Normal Human Adults? Biochim. Biophys. Acta 18, 576 (1955).

    Article  CAS  Google Scholar 

  56. Huisman, T. H. J., E. A. Martis and A. Dozy: Chromatography of Hemoglobin Types on Carboxymethylcellulose. J. Lab. Clin. Med. 52, 312 (1958) [Chem. Abstr. 52, 17361 (1958)].

    Google Scholar 

  57. a. Hunt, J. A.: The Identity of the IX Chains of Adult and Foetal Human Haemoglobins. Nature (London) (in press).

    Google Scholar 

  58. Hunt, J. A. and V. M. Ingram: Abnormal Human Haemoglobins. II. The Chymotryptic Digestion of the Trypsin-Resistant “Core” of Haemoglobins A and S. Biochim. Biophys. Acta 28, 546 (1958).

    Article  CAS  Google Scholar 

  59. Hunt, J. A. and V. M. Ingram: Allelomorphism and the Chemical Differences of the Human Haemoglobins A, S, and C. Nature (London) 181, 1062 (1958).

    Article  CAS  Google Scholar 

  60. Hutchinson, W. D. and J. Vinograd: unpublished.

    Google Scholar 

  61. Ingbar, S. H. and E. H. Kass: Sulfhydryl Content of Normal Hemoglobin and Hemoglobin in Sickle-cell Anemia. Proc. Soc. exp. Biol. Med. 77, 74 (1951)

    CAS  Google Scholar 

  62. Ingram, D. J. E., J. F. Gibson and M. F. Perutz: Electron Spin Resonance in Myoglobin and Haemoglobin. Orientation of the four Haem Groups in Haemoglobin. Nature (London) 178, 905 (1956).

    Article  CAS  Google Scholar 

  63. Ingram, V. M.: Sulfhydryl Groups in Haemoglobins. Biochemic. J. 59, 653 (1955).

    CAS  Google Scholar 

  64. Ingram, V. M.: A Specific Chemical Difference Between the Globins of Normal Human and Sickle-cell Anaemia Haemoglobin. Nature (London) 178, 792 (1956).

    Article  CAS  Google Scholar 

  65. Ingram, V. M.: Gene Mutations in Human Haemoglobin: The Chemical Difference between Normal and Sickle Cell Haemoglobin. Nature (London) 180, 326 (1957)

    Article  CAS  Google Scholar 

  66. Ingram, V. M.: The Sulfhydryl Groups of Sickle-cell Haemoglobin. Biochemic. J. 65, 760 (1957).

    CAS  Google Scholar 

  67. Ingram, V. M.: Abnormal Human Haemoglobins. I. The Comparison of Normal Human and Sickle-cell Haemoglobins by “Fingerprinting”. Biochim. Biophys. Acta s, 539 (1958).

    Google Scholar 

  68. Ingram, V. M.: The Chemical Difference between Normal Human and Sickle Cell Anaemia Haemoglobins. In: Conference on Hemoglobin. Nat. Acad. Sci., National Research Council, Washington, D. C., Publication No. 557, 1958, p. 233.

    Google Scholar 

  69. a. Ingram, V. M.: Private communication.

    Google Scholar 

  70. Itano, H. A.: Human Hemoglobin. Science (Washington) 117, 89 (1953).

    Article  CAS  Google Scholar 

  71. Itano, H. A.: Clinical States Associated with Alteration of the Hemoglobin Molecule. Arch. Internal Med. 96, 287 (1955) [Chem. Abstr. 50, 2834 (1956)]

    Google Scholar 

  72. Itano, H. A.: The Hemoglobins. Annu. Rev. Biochem. 25, 331 (1956).

    Article  CAS  Google Scholar 

  73. Itano, H. A.: The Human Hemoglobins: Their Properties and Genetic Control. Adv. Protein Chem. 12, 215 (1957)

    Article  CAS  Google Scholar 

  74. Itano, H. A.: Asymmetric Dissociation and Hybridization of Hemoglobin Molecules. Correlation with Chemical and Genetic Subunits. Abstr., Meeting Amer. Chem. Soc., Sept. 1958.

    Google Scholar 

  75. Itano, H. A., W. R. Bergren and P. Sturgeon: The Abnormal Human Hemoglobins. Medicine 35, 121 (1956).

    Article  CAS  Google Scholar 

  76. Jones, R. T. and W. A. Schroeder: unpublished.

    Google Scholar 

  77. Jonxis, J. H. P.: Foetal Haemoglobin and Rh Antagonisms. In: F. J. W. Roughton and J. C. Kendrew, Haemoglobin, p. 261. London: Butterworths, and New York: Interscience Publ. 1949.

    Google Scholar 

  78. Jonxis, J. H. P. and T. H. J. Huisman: The Detection and Estimation of Fetal Hemoglobin by Means of the Alkali Denaturation Test. Blood 11, 1009 (1956).

    Google Scholar 

  79. Jope, E. M.: The Ultraviolet Spectral Absorption of Haemoglobins Inside and Outside the Red Blood Cell. In: F. J. W. Roughton and J. C. Kendrew, Haemoglobin, p. 205. London: Butterworths, New York: Interscience. 1949.

    Google Scholar 

  80. Jope, H. M. and J. R. P. O’Brien: Crystallization and Solubility Studies on Human Adult and Foetal Haemoglobins. In: F. J. W. Roughton and J. C. Kendrew, Haemoglobin, p. 269. London: Butterworths, and New York: Interscience Publ. 1949.

    Google Scholar 

  81. Kauffmann, T. und F.-P. Boettcher: Bestimmung der C-terminalen Aminosäuren von Menschen-, Pferde- und Rinderhämoglobin. Z. Naturf. 136, 467 (1958).

    Google Scholar 

  82. Keilin, D.: A Comparative Study of Turacin and Haematin and its Bearing on Cytochrome. Proc. Roy. Soc. (London) 100 B, 129 (1926).

    Google Scholar 

  83. Kleinknecht, R.: Das Vorkommen der mittels Alkalidenaturierung unter-scheidbaren Hämoglobintypen Hb, Hbg und Hbg im Säuglingsalter. Monatsschr. Kinderheilk. 101, 360 (1953)

    CAS  Google Scholar 

  84. a. Kon, H. and N. Davidson: Nuclear Magnetic Relaxation of Water Protons by Ferrihemoglobin and Ferrimyoglobin. J. Molecular Biol. (1959) (in press).

    Google Scholar 

  85. Körber, E.: Über Differenzen des Blutfarbstoffes. Dissert., Dorpat, 1866.

    Google Scholar 

  86. Kunkel, H. G., R. Ceppellini, O. Muller-Eberhard and J. Wolf: The Minor Basic Hemoglobin (Hb) Component in the Blood of Normal Individuals and Patients with Thalassemia. J. Clin. Investigation 36, 1615 (1957)

    Article  CAS  Google Scholar 

  87. Kunkel, H. G. and G. Wallenius: New Hemoglobin in Normal Adult Blood. Science (Washington) 122, 288 (1955).

    Article  CAS  Google Scholar 

  88. Künzer, W.: Human Embryo Haemoglobins. Nature (London) 179, 477 (1957).

    Article  Google Scholar 

  89. Küster, W. und G. F. Koppenhöfer: Über den Blutfarbstoff. Z. physiol. Chem. (Hoppe-Seyler) 170, 106 (1927).

    Google Scholar 

  90. Lamm, O. and A. Polson: The Determination of Diffusion Constants of Proteins by a Refractometric Method. Biochemic. J. 30, 528 (1936).

    CAS  Google Scholar 

  91. Lemberg, R. and J. W. Legge: Hematin Compounds and Bile Pigments: Their Constitution, Metabolism, and Function. New York: Interscience Publ. 1949

    Book  Google Scholar 

  92. Masri, M. S. and K. Singer: Studies on Abnormal Hemoglobins. XII. Terminal and Free Amino Groups of Various Types of Human Hemoglobins. Arch. Biochem. Biophys. 58, 414 (1955).

    Article  CAS  Google Scholar 

  93. Matsuda, G. and W. A. Schroeder: unpublished.

    Google Scholar 

  94. Matsuda, G., R. Shelton and W. A. Schroeder: unpublished.

    Google Scholar 

  95. Moore, D. H. and L. Reiner: Electrophoretic and Ultracentrifugal Analyses of Globin Components. J. Biol. Chem. 156, 411 (1944).

    CAS  Google Scholar 

  96. Morrison, D. B. and A. Hisey: The Carbon Monoxide Capacity, Iron, and Total Nitrogen of Dog Hemoglobin. J. Biol. Chem. 109, 233 (1935).

    CAS  Google Scholar 

  97. Morrison, M.: Discussion in: Conference on Hemoglobin. Nat. Acad. Sci., National Research Council, Washington, D. C., Publication No. 557, 1958, p. 166.

    Google Scholar 

  98. Morrison, M. and J. L. Cook: Chromatographic Fractionation of Normal Adult Oxyhemoglobin. Science (Washington) 122, 920 (1955).

    Article  CAS  Google Scholar 

  99. Murayama, M.: Titratable Sulfhydryl Groups of Normal and Sickle-cell Hemoglobins at 0° and 38°. J. Biol. Chem. 228, 231 (1957).

    CAS  Google Scholar 

  100. Titratable Sulfhydryl Groups of Hemoglobin C and Fetal Hemoglobin at 0° and 38°. J. Biol. Chem. 230, 163 (1958).

    Google Scholar 

  101. Patchornik, A., W. B. Lawson and B. Witkop: Selective Cleavage of Peptide Bonds. II. The Tryptophyl Peptide Bond and the Cleavage of Glucagon. J. Amer. Chem. Soc. 80, 4747 (1958).

    Article  CAS  Google Scholar 

  102. Pauling, L.: Abnormality of Hemoglobin Molecules in Hereditary Hemolytic Anemias. Harvey Lect. 49, 216 (1953/54).

    Google Scholar 

  103. Pauling, L. and C. D. Coryell: The Magnetic Properties and Structure of Hemoglobin, Oxyhemoglobin and Carbonmonoxyhemoglobin. Proc. Nat. Acad. Sci. (USA) 22, 210 (1936).

    Article  CAS  Google Scholar 

  104. Pauling, L., H. A. Itano, S. J. Singer and I. C. Wells: Sickle Cell Anemia, a Molecular Disease. Science (Washington) no, 2865 (1949)

    Google Scholar 

  105. Perutz, M. F., I. F. Trotter, E. R. Howells and D. W. Green: An X-Ray Study of Reduced Human Hemoglobin. Acta Cristallogr. 8, 241 (1955).

    Article  CAS  Google Scholar 

  106. Porter, R. R. and F. Sanger: The Free Amino Groups of Haemoglobins. Biochemic. J. 42, 287 (1948).

    CAS  Google Scholar 

  107. Prins, H. K. and T. H. J. Huisman: Chromatographic Behaviour of Haemoglobin E. Nature (London) 177, 840 (1956).

    Article  CAS  Google Scholar 

  108. Rhinesmith, H. S., W. A. Schroeder and N. Martin: The N-Terminal Sequence of the Chains of Normal Adult Human Hemoglobin. J. Amer. Chem. Soc. 80, 3358 (1958).

    Article  CAS  Google Scholar 

  109. Rhinesmith, H. S., W. A. Schroeder and L. Pauling: The N-Terminal Amino Acid Residues of Normal Adult Human Hemoglobin: A Quantitative Study of Certain Aspects of Sanger’s DNP-Method. J. Amer. Chem. Soc. 79, 609 (1957)

    Article  CAS  Google Scholar 

  110. Rhinesmith, H. S., W. A. Schroeder and L. Pauling: A Quantitative Study of the Hydrolysis of Human Dinitrophenyl-(DNP)globin: The Number and Kind of Polypeptide Chains in Normal Adult Human Hemoglobin. J. Amer. Chem. Soc. 79, 4682 (1957).

    Article  CAS  Google Scholar 

  111. Riggs, A. F.: Sulfhydryl Groups and the Interaction between the Hemes in Hemoglobin. J. Gen. Physiol. 36, 1 (1952).

    Article  CAS  Google Scholar 

  112. Rossi-Fanelli, A., E. Antonini and A. Caputo: Pure Native Globin from Human Haemoglobin: Preparation and Some Physico-chemical Properties. Biochim. Biophys. Acta 28, 221 (1958).

    Article  CAS  Google Scholar 

  113. Rossi-Fanelli, A., D. Cavallini and C. De Marco: Amino Acid Composition of Human Crystallized Myoglobin and Haemoglobin. Biochim. Biophys. Acta 17, 377 (1955).

    Article  CAS  Google Scholar 

  114. Rossi-Fanelli, A., D. Cavallini, C. De Marco and F. Trasatti: Fetal Hb. I. Quantitative Analysis of the Amino Acids of Crystalline Human Fetal Hb and Some Technical Precautions. Boll. Soc. ital. Biol. sper. 31, 328 (1955) [Chem. Abstr. 49, 14982 (1955)].

    Google Scholar 

  115. Roughton, F. J. W. and J. C. Kendrew (Editors): Haemoglobin. London: Butterworths, and New York: Interscience Publ. 1949

    Google Scholar 

  116. Sanger, F.: The Arrangement of Amino Acids in Proteins. Adv. Protein Chem. 7, 1 (1952).

    Article  CAS  Google Scholar 

  117. Schapira, G. et J.-C. Dreyfus: Groupes N-terminaux de l’hémoglobine de la maladie de Cooley. C. R. Séances Soc. Biol. 148, 895 (1954)

    Google Scholar 

  118. Schräm, E., S. Moore and E. J. Bigwood: Chromatographie Determination of Cystine as Cysteic Acid. Biochemic. J. 57, 33 (1954)

    Google Scholar 

  119. Schramm, G., J. W. Schneider und A. Anderer: Zur Bestimmung der Amino-Endgruppen verschiedener Hämoglobine und des Tabakmosaikvirus mit Phenylisothiocyanat. Z. Naturforsch, iib, 12 (1956) [Chem. Abstr. 50, 8789 (1956)].

    Google Scholar 

  120. Schroeder, W. A. and J. Balog: unpublished.

    Google Scholar 

  121. Schroeder, W. A. and L. M. Kay: unpublished.

    Google Scholar 

  122. Schroeder, W. A., L. M. Kay and I. C. Wells: Amino Acid Composition of Hemoglobins of Normal Negores and Sickle-cell Anemics. J. Biol. Chem. 187, 221 (1950)

    CAS  Google Scholar 

  123. Schroeder, W. A. and G. Matsuda: N-Terminal Residues of Human Fetal Hemoglobin. J. Amer. Chem. Soc. 80, 1521 (1958).

    Article  CAS  Google Scholar 

  124. Schroeder, W. A., G. Matsuda and R. T. Jones: unpublished.

    Google Scholar 

  125. Schroeder, W. A., G. Matsuda, N. Martin, L. M. Kay and M. Clegg: unpublished.

    Google Scholar 

  126. Stein, W. H., H. G. Kunkel, R. D. Cole, D. H. Spackman and S. Moore: Observations on the Amino Acid Composition of Human Hemoglobins. Biochim. Biophys. Acta 24, 640 (1957)

    Article  CAS  Google Scholar 

  127. Svedberg, T. and K. O. Pedersen: The Ultracentrifuge. Oxford: Clarendon Press. 1940.

    Google Scholar 

  128. Taylor, J. F. and R. L. Swarm: Molecular Weight of Human Fetal Hemoglobin. Federat. Proc. (Amer. Soc. exp. Biol.) 8, 259 (1949)

    Google Scholar 

  129. Theorell, H.: Über die chemische Konstitution des Cytochroms c. Biochem. Z. 298, 242 (1938).

    CAS  Google Scholar 

  130. Theorell, H.: Cystin aus Porphyrin C. Enzymologia 6, 88 (1939).

    CAS  Google Scholar 

  131. Relations between Prosthetic Groups, Coenzymes and Enzymes. In: D. E. Green, Currents in Biochemical Research, p. 275. New York: Interscience Publ. 1956.

    Google Scholar 

  132. Tuppy, H. and S. Paleus: Study of a Peptic Degradation Product of Cytochrome c. I. Purification and Chemical Composition. Acta Chem. Scand. 9, 353 (1955).

    Article  CAS  Google Scholar 

  133. Tuttle, A. H.: Human Hemoglobins. J. Chronic Diseases 6, 528 (1957) [Chem. Abstr. 52, 2226 (1958)].

    Google Scholar 

  134. Van Der Schaaf, P. C. and T. H. J. Huisman: The Amino Acid Composition of Human Adult and Foetal Carbonmonoxyhaemoglobin Estimated by Ion Exchange Chromatography. Biochim. Biophys. Acta 17, 81 (1955).

    Google Scholar 

  135. Vinograd, J. and U. Hasserodt: unpublished.

    Google Scholar 

  136. Vinograd, J. and W. D. Hutchinson: C-Hybrids of Human Hemoglobins. I. Dissociation of Human Haemoglobin and the Isolation of C-Labelled Haemoglobin Hybrids. Nature (London) (submitted).

    Google Scholar 

  137. Vinograd, J. R., W. D. Hutchinson and W. A. Schroeder: C-Hybrids of Human Hemoglobins. II. The Identification of the Aberrant Chain in Human Hemoglobin S. J. Amer. Chem. Soc. (in press).

    Google Scholar 

  138. Walker, J. and E. P. N. Turnbull: Hemoglobin and Red Cells in the Human Fetus, in. Fetal and Adult Hemoglobin. Arch. Disease Childhood 30, III (1955) [Chem. Abstr. 49, 11125 (1955)]

    Google Scholar 

  139. Wilson, S. and D. B. Smith: Separation of the Valyl-leucyl- and Valyl-glutamyl-polypeptide Components of Horse Globin by Column Chromatography and Fractional Precipitation. Can. J. Biochem. Physiol. 37, 405 (1959).

    Article  CAS  Google Scholar 

  140. Wyman, J., Jr.: Heme Proteins. Adv. Protein Chem. 4, 407 (1948).

    Article  CAS  Google Scholar 

  141. Zinsser, H. H. and Y.-C. Tang: X-Ray Observations on Single Crystals of Carbonmonoxyhemoglobin from Human Fetal Blood. Arch. Biochem. Biophys. 34, 81 (1951)

    Article  CAS  Google Scholar 

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Schroeder, W.A. (1959). The Chemical Structure of the Normal Human Hemoglobins. In: Zechmeister, L. (eds) Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products / Progrès dans la Chimie des Substances Organiques Naturelles. Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products / Progrès dans la Chimie des Substances Organiques Naturelles, vol 17. Springer, Vienna. https://doi.org/10.1007/978-3-7091-8052-5_7

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  • DOI: https://doi.org/10.1007/978-3-7091-8052-5_7

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