248
AUSTEN RIGGS
of red cell hemolysates analyzed in cacodylate buffers. Arch. Biochem. Biophys.
106,433.
Chanutin, A., and Curnish, R. (1967). Effect of organic and inorganic phosphates
on the oxygen equilibrium of human erythrocytes. Arch. Biochem. Biophys. 121,
96.
Chiancone, E., Vecchini, P., Forlani, L., Antonini, E., and Wyman, J. (1966).
Dissociation of hemoglobin from different animal species into subunits. Biochim.
Biophys. Acta 127, 549.
Christomanos, A. (1964). Zur Kenntnis des Hamoglobins des Sagebarsches (Serranus
gobrilla). 11. Enzymologia 27, 199.
Christomanos, A., and Pavlopulu, C. (1967). Zur Konstitution der Hamoglobine der
Su.swasserschildkrote clemys caspica rioulata und Die des Aals Anguilla anguilla.
Folia Biochim. Biol. Graeca 4, 24.
Cokelet, G., and Meiselman, H. J. (1968). Rheological comparison of hemoglobin
solutions and erythrocyte suspensions. Science 162, 275.
Dayhoff, M. (1969). “Atlas of Protein Sequence and Structure.” Natl. Biomed. Res.
Found., Silver Spring, Maryland.
Dixon, G. (1966). Mechanisms of protein evolution. Essays Biochem. 2, 148.
Eguchi, H., Hashimoto, K., and Matsuura, F. (1960). Comparative studies on two
hemoglobins of salmon. 111. Amino acid composition. Bull. lapan. SOC. Sci.
Fisherier 26, 810.
Enoki, Y., and Tyuma, I. (1964). Further studies on hemoglobin-oxygen equilibrium.
Japan. J . Physiol. 14, 280.
Fange, H. (1966). Physiology of the swimbladder. Physiol. Reu. 46, 299.
Gratzer, W., and Allison, A. (1960). Multiple haemoglobins. Biol. Rev. 35, 459.
Green, A,, and Root, R. (1933). The equilibrium between hemoglobin and oxygen
Guidotti, G., Konigsberg, W., and Craig, L. (1963). On the dissociation of normal
Haldane, J. (1922). “Respiration,” p. 72. Yale Univ. Press, New Haven, Connecticut.
Hashimoto, K., and Matsuura, F. ( 1959a). Comparative studies on two hemoglobins
of salmon. Bull. Japan. SOC. Sci. Fisheries 24, 724.
Hashimoto, K., and Matsuura, F. (19595). Comparative studies on two hemoglobins
of salmon. 11. Crystallization and some physical properties. Bull. Japan. SOC. Sci.
Fisheries 25, 465.
Hashimoto, K., and Matsuura, F. (1960a). Multiple hemoglobins in fish. 11. Bull.
Japan. SOC. Sci. Fisheries 26, 354.
Hashimoto, K., and Matsuura, F. (1960b). Comparative studies on two hernoglobins
of salmon. V. Change in proportion of two hemoglobins with growth. Bull. Japan.
SOC. Sci. Fisheries 26, 931.
Hashinioto, K., and Matsuura, F. (1962). Comparative studies on two hemoglobins
of salmon. VI. N-terminal amino acid. Bull. Japan. SOC. Sci. Fisheries 28, 914.
Hashimoto, K., Yamaguchi, Y., and Matsuura, F. (1960). Comparative studies on
two hemoglobins of salmon. IV. Oxygen dissociation curve. Bull. Japan. SOC.
Sci. Fisheries 26, 827.
Herner, A,, and Frieden, E. (1961). Biochemical changes during anuran metamorphosis. VIII. Changes in the nature of red cell proteins. Arch. Biochem.
Biophys. 95, 25.
Hill, R., and Davis, R. (1967). The pK of specific groups of proteins. I. The a-amino
group of the ( I chain of human CO-hemoglobin. J . Biol. Chem. 242, 2005.
in the blood of certain fishes. Biol. Bull. 64, 383.
adult human hemoglobin. Proc. Natl. Acad. Sci. U.S. 50, 774.
AUSTEN RIGGS
of red cell hemolysates analyzed in cacodylate buffers. Arch. Biochem. Biophys.
106,433.
Chanutin, A., and Curnish, R. (1967). Effect of organic and inorganic phosphates
on the oxygen equilibrium of human erythrocytes. Arch. Biochem. Biophys. 121,
96.
Chiancone, E., Vecchini, P., Forlani, L., Antonini, E., and Wyman, J. (1966).
Dissociation of hemoglobin from different animal species into subunits. Biochim.
Biophys. Acta 127, 549.
Christomanos, A. (1964). Zur Kenntnis des Hamoglobins des Sagebarsches (Serranus
gobrilla). 11. Enzymologia 27, 199.
Christomanos, A., and Pavlopulu, C. (1967). Zur Konstitution der Hamoglobine der
Su.swasserschildkrote clemys caspica rioulata und Die des Aals Anguilla anguilla.
Folia Biochim. Biol. Graeca 4, 24.
Cokelet, G., and Meiselman, H. J. (1968). Rheological comparison of hemoglobin
solutions and erythrocyte suspensions. Science 162, 275.
Dayhoff, M. (1969). “Atlas of Protein Sequence and Structure.” Natl. Biomed. Res.
Found., Silver Spring, Maryland.
Dixon, G. (1966). Mechanisms of protein evolution. Essays Biochem. 2, 148.
Eguchi, H., Hashimoto, K., and Matsuura, F. (1960). Comparative studies on two
hemoglobins of salmon. 111. Amino acid composition. Bull. lapan. SOC. Sci.
Fisherier 26, 810.
Enoki, Y., and Tyuma, I. (1964). Further studies on hemoglobin-oxygen equilibrium.
Japan. J . Physiol. 14, 280.
Fange, H. (1966). Physiology of the swimbladder. Physiol. Reu. 46, 299.
Gratzer, W., and Allison, A. (1960). Multiple haemoglobins. Biol. Rev. 35, 459.
Green, A,, and Root, R. (1933). The equilibrium between hemoglobin and oxygen
Guidotti, G., Konigsberg, W., and Craig, L. (1963). On the dissociation of normal
Haldane, J. (1922). “Respiration,” p. 72. Yale Univ. Press, New Haven, Connecticut.
Hashimoto, K., and Matsuura, F. ( 1959a). Comparative studies on two hemoglobins
of salmon. Bull. Japan. SOC. Sci. Fisheries 24, 724.
Hashimoto, K., and Matsuura, F. (19595). Comparative studies on two hemoglobins
of salmon. 11. Crystallization and some physical properties. Bull. Japan. SOC. Sci.
Fisheries 25, 465.
Hashimoto, K., and Matsuura, F. (1960a). Multiple hemoglobins in fish. 11. Bull.
Japan. SOC. Sci. Fisheries 26, 354.
Hashimoto, K., and Matsuura, F. (1960b). Comparative studies on two hernoglobins
of salmon. V. Change in proportion of two hemoglobins with growth. Bull. Japan.
SOC. Sci. Fisheries 26, 931.
Hashinioto, K., and Matsuura, F. (1962). Comparative studies on two hemoglobins
of salmon. VI. N-terminal amino acid. Bull. Japan. SOC. Sci. Fisheries 28, 914.
Hashimoto, K., Yamaguchi, Y., and Matsuura, F. (1960). Comparative studies on
two hemoglobins of salmon. IV. Oxygen dissociation curve. Bull. Japan. SOC.
Sci. Fisheries 26, 827.
Herner, A,, and Frieden, E. (1961). Biochemical changes during anuran metamorphosis. VIII. Changes in the nature of red cell proteins. Arch. Biochem.
Biophys. 95, 25.
Hill, R., and Davis, R. (1967). The pK of specific groups of proteins. I. The a-amino
group of the ( I chain of human CO-hemoglobin. J . Biol. Chem. 242, 2005.
in the blood of certain fishes. Biol. Bull. 64, 383.
adult human hemoglobin. Proc. Natl. Acad. Sci. U.S. 50, 774.