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.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Adair, G. S.: A Comparison of the Molecular Weights of the Proteins. Proc. Cambridge Phil. Soc. 1, 75 (1924).
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).
Allen, D. W., K. F. Guthe and J. Wyman, Jr.: Further Studies on the Oxygen Equilibrium of Hemoglobin. J. Biol. Chem. 187, 393 (1950).
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)
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).
Allison, A. C.: Notation for Hemoglobin Types and Genes Controlling Their Synthesis. Science (Washington) 122, 640 (1955).
Allison, A. C. and R. Cecil: The Thiol Groups of Normal Adult Human Haemoglobin. Biochemic. J. 69, 27 (1958).
Anonymous: Statement Concerning a System of Nomenclature for the Varieties of Human Hemoglobin. Blood 8, 386 (1953).
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).
Bangham, A. D. and H. Lehmann: “Multiple” Haemoglobins in the Horse. Nature (London) 181, 267 (1958).
Barrett, H. W. and W. A. Schroeder: unpublished.
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).
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)
Bernhart, F. W. and L. Skeggs: The Iron Content of Crystalline Human Hemoglobin. J. Biol. Chem. 147, 19 (1943).
Betke, K.: Der menschUche rote Blutfarbstoff bei Fetus und reifem Organismus. Berlin: Springer-Verlag. 1954
Bragg, W. L. and M. F. Perutz: The External Form of the Hemoglobin Molecule. II. Acta Crystallogr. 5, 323 (1952).
Brown, H.: The Free Amino Groups and Terminal Dipeptides of Human Adult Hemoglobin. Arch. Biochem. Biophys. 61, 241 (1956).
The Sulfur Distribution and Some Cysteic Acid Peptides of Human Adult Hemoglobin. Arch. Biochem. Biophys. 67, 256 (1957).
Cabannes, R. et CH. Serain: Étude électrophorétique des hémoglobines des Mammifères domestiques d’Algérie. C. R. Séances Soc. Biol. 149, 1193 (1955)
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.
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.
Clegg, M. and W. A. Schroeder: J. Amer. Chem. Soc. (1959)
Cole, R. D., W. H. Stein and S. Moore: On the Cysteine Content of Human Hemoglobin. J. Biol. Chem. 233, 1359 (1958).
Conference on Hemoglobin. Nat. Acad. Sci., National Research Council, Washington, D. C., Publication No. 557, 1958.
Cook, J. L. and M. Morrison: Ion Exchange Chromatography of Human Hemoglobin. Federat. Proc. (Amer. Soc. exp. Biol.) 15, 235 (1956).
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)
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)
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.
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.
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.
Dickman, S. R. and I. H. Moncrief: Primary Amide Groups of Human Hemoglobin. Proc. Soc. exp. Biol. Med. 77, 631 (1951).
Drabkin, D. L.: Metabolism of the Hemin Chromoproteins. Physiol. Rev. 31, 345 (1951).
Drabkin, D. L.: Symposium on Molecular Heterogeneity of Hemoglobin. Federat. Proc. (Amer. Soc. exp. Biol.) 16, 740–773 (1957)
Heredity and Environment in Structure of Hemoglobin. Federat. Proc. (Amer. Soc. exp. Biol.) 16, 740 (1957).
Drescher, H. und W. Künzer: Der Blutfarbstoff der menschlichen Feten. Klin. Wschr. 32, 92 (1954).
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).
Eastman, N. J.: Obstetrics. loth ed., p. 168. New York: Appleton-Century- Crofts. 1950.
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)
Field, E. O. and J. R. P. O’Brien: Dissociation of Human Haemoglobin at Low pH. Biochemic. J. 60, 656 (1955).
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.
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).
Halbrecht, I. and C. Klibanski: Identification of a New Normal Embryonic Haemoglobin. Nature (London) 178, 794 (1956).
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)].
Hasserodt, U. and M. Clegg: unpublished.
Hasserodt, U. and J. Vinograd: Dissociation of Human Carbonmonoxy- hemoglobin at High pH. Proc. Nat. Acad. Sei. (USA) 45, 12 (1959)
Hasserodt, U., J. Vinograd and R. Srinivasan: The Molecular Weight of Human Hemoglobin. J. Amer. Chem. Soc. (in press).
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.
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).
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)
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).
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)
Huisman, T. H. J.: Abnormal Hemoglobins. Chn. Chim. Acta 3, 201 (1958).
Huisman, T. H. J. and A. Dozy: The Action of Carboxypeptidase on Different Human Haemoglobins. Biochim. Biophys. Acta 20, 400 (1956).
Huisman, T. H. J. and J. Drinkwaard: The N-terminal Residues of Five Different Human Haemoglobins. Biochim. Biophys. Acta 18, 588 (1955).
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).
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)].
a. Hunt, J. A.: The Identity of the IX Chains of Adult and Foetal Human Haemoglobins. Nature (London) (in press).
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).
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).
Hutchinson, W. D. and J. Vinograd: unpublished.
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)
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).
Ingram, V. M.: Sulfhydryl Groups in Haemoglobins. Biochemic. J. 59, 653 (1955).
Ingram, V. M.: A Specific Chemical Difference Between the Globins of Normal Human and Sickle-cell Anaemia Haemoglobin. Nature (London) 178, 792 (1956).
Ingram, V. M.: Gene Mutations in Human Haemoglobin: The Chemical Difference between Normal and Sickle Cell Haemoglobin. Nature (London) 180, 326 (1957)
Ingram, V. M.: The Sulfhydryl Groups of Sickle-cell Haemoglobin. Biochemic. J. 65, 760 (1957).
Ingram, V. M.: Abnormal Human Haemoglobins. I. The Comparison of Normal Human and Sickle-cell Haemoglobins by “Fingerprinting”. Biochim. Biophys. Acta s, 539 (1958).
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.
a. Ingram, V. M.: Private communication.
Itano, H. A.: Human Hemoglobin. Science (Washington) 117, 89 (1953).
Itano, H. A.: Clinical States Associated with Alteration of the Hemoglobin Molecule. Arch. Internal Med. 96, 287 (1955) [Chem. Abstr. 50, 2834 (1956)]
Itano, H. A.: The Hemoglobins. Annu. Rev. Biochem. 25, 331 (1956).
Itano, H. A.: The Human Hemoglobins: Their Properties and Genetic Control. Adv. Protein Chem. 12, 215 (1957)
Itano, H. A.: Asymmetric Dissociation and Hybridization of Hemoglobin Molecules. Correlation with Chemical and Genetic Subunits. Abstr., Meeting Amer. Chem. Soc., Sept. 1958.
Itano, H. A., W. R. Bergren and P. Sturgeon: The Abnormal Human Hemoglobins. Medicine 35, 121 (1956).
Jones, R. T. and W. A. Schroeder: unpublished.
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.
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).
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.
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.
Kauffmann, T. und F.-P. Boettcher: Bestimmung der C-terminalen Aminosäuren von Menschen-, Pferde- und Rinderhämoglobin. Z. Naturf. 136, 467 (1958).
Keilin, D.: A Comparative Study of Turacin and Haematin and its Bearing on Cytochrome. Proc. Roy. Soc. (London) 100 B, 129 (1926).
Kleinknecht, R.: Das Vorkommen der mittels Alkalidenaturierung unter-scheidbaren Hämoglobintypen Hb, Hbg und Hbg im Säuglingsalter. Monatsschr. Kinderheilk. 101, 360 (1953)
a. Kon, H. and N. Davidson: Nuclear Magnetic Relaxation of Water Protons by Ferrihemoglobin and Ferrimyoglobin. J. Molecular Biol. (1959) (in press).
Körber, E.: Über Differenzen des Blutfarbstoffes. Dissert., Dorpat, 1866.
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)
Kunkel, H. G. and G. Wallenius: New Hemoglobin in Normal Adult Blood. Science (Washington) 122, 288 (1955).
Künzer, W.: Human Embryo Haemoglobins. Nature (London) 179, 477 (1957).
Küster, W. und G. F. Koppenhöfer: Über den Blutfarbstoff. Z. physiol. Chem. (Hoppe-Seyler) 170, 106 (1927).
Lamm, O. and A. Polson: The Determination of Diffusion Constants of Proteins by a Refractometric Method. Biochemic. J. 30, 528 (1936).
Lemberg, R. and J. W. Legge: Hematin Compounds and Bile Pigments: Their Constitution, Metabolism, and Function. New York: Interscience Publ. 1949
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).
Matsuda, G. and W. A. Schroeder: unpublished.
Matsuda, G., R. Shelton and W. A. Schroeder: unpublished.
Moore, D. H. and L. Reiner: Electrophoretic and Ultracentrifugal Analyses of Globin Components. J. Biol. Chem. 156, 411 (1944).
Morrison, D. B. and A. Hisey: The Carbon Monoxide Capacity, Iron, and Total Nitrogen of Dog Hemoglobin. J. Biol. Chem. 109, 233 (1935).
Morrison, M.: Discussion in: Conference on Hemoglobin. Nat. Acad. Sci., National Research Council, Washington, D. C., Publication No. 557, 1958, p. 166.
Morrison, M. and J. L. Cook: Chromatographic Fractionation of Normal Adult Oxyhemoglobin. Science (Washington) 122, 920 (1955).
Murayama, M.: Titratable Sulfhydryl Groups of Normal and Sickle-cell Hemoglobins at 0° and 38°. J. Biol. Chem. 228, 231 (1957).
Titratable Sulfhydryl Groups of Hemoglobin C and Fetal Hemoglobin at 0° and 38°. J. Biol. Chem. 230, 163 (1958).
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).
Pauling, L.: Abnormality of Hemoglobin Molecules in Hereditary Hemolytic Anemias. Harvey Lect. 49, 216 (1953/54).
Pauling, L. and C. D. Coryell: The Magnetic Properties and Structure of Hemoglobin, Oxyhemoglobin and Carbonmonoxyhemoglobin. Proc. Nat. Acad. Sci. (USA) 22, 210 (1936).
Pauling, L., H. A. Itano, S. J. Singer and I. C. Wells: Sickle Cell Anemia, a Molecular Disease. Science (Washington) no, 2865 (1949)
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).
Porter, R. R. and F. Sanger: The Free Amino Groups of Haemoglobins. Biochemic. J. 42, 287 (1948).
Prins, H. K. and T. H. J. Huisman: Chromatographic Behaviour of Haemoglobin E. Nature (London) 177, 840 (1956).
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).
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)
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).
Riggs, A. F.: Sulfhydryl Groups and the Interaction between the Hemes in Hemoglobin. J. Gen. Physiol. 36, 1 (1952).
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).
Rossi-Fanelli, A., D. Cavallini and C. De Marco: Amino Acid Composition of Human Crystallized Myoglobin and Haemoglobin. Biochim. Biophys. Acta 17, 377 (1955).
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)].
Roughton, F. J. W. and J. C. Kendrew (Editors): Haemoglobin. London: Butterworths, and New York: Interscience Publ. 1949
Sanger, F.: The Arrangement of Amino Acids in Proteins. Adv. Protein Chem. 7, 1 (1952).
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)
Schräm, E., S. Moore and E. J. Bigwood: Chromatographie Determination of Cystine as Cysteic Acid. Biochemic. J. 57, 33 (1954)
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)].
Schroeder, W. A. and J. Balog: unpublished.
Schroeder, W. A. and L. M. Kay: unpublished.
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)
Schroeder, W. A. and G. Matsuda: N-Terminal Residues of Human Fetal Hemoglobin. J. Amer. Chem. Soc. 80, 1521 (1958).
Schroeder, W. A., G. Matsuda and R. T. Jones: unpublished.
Schroeder, W. A., G. Matsuda, N. Martin, L. M. Kay and M. Clegg: unpublished.
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)
Svedberg, T. and K. O. Pedersen: The Ultracentrifuge. Oxford: Clarendon Press. 1940.
Taylor, J. F. and R. L. Swarm: Molecular Weight of Human Fetal Hemoglobin. Federat. Proc. (Amer. Soc. exp. Biol.) 8, 259 (1949)
Theorell, H.: Über die chemische Konstitution des Cytochroms c. Biochem. Z. 298, 242 (1938).
Theorell, H.: Cystin aus Porphyrin C. Enzymologia 6, 88 (1939).
Relations between Prosthetic Groups, Coenzymes and Enzymes. In: D. E. Green, Currents in Biochemical Research, p. 275. New York: Interscience Publ. 1956.
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).
Tuttle, A. H.: Human Hemoglobins. J. Chronic Diseases 6, 528 (1957) [Chem. Abstr. 52, 2226 (1958)].
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).
Vinograd, J. and U. Hasserodt: unpublished.
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).
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).
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)]
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).
Wyman, J., Jr.: Heme Proteins. Adv. Protein Chem. 4, 407 (1948).
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)
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1959 Springer-Verlag in Vienna
About this chapter
Cite this chapter
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
Download citation
DOI: https://doi.org/10.1007/978-3-7091-8052-5_7
Publisher Name: Springer, Vienna
Print ISBN: 978-3-7091-8054-9
Online ISBN: 978-3-7091-8052-5
eBook Packages: Springer Book Archive