Skip to main content
SpringerLink
Log in

The transferrins

  • Conference paper
  • First Online:
Structure And Bonding

Part of the book series: Structure and Bonding ((STRUCTURE,volume 1))

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Aasa, R., B. G. Malmstrom, P. Saltman, and T. Vanngard: The specific binding of iron (III) and copper (II) to transferrin and conalbumin. Biochim. Biophys. Acta 75, 203 (1963).

    CAS  Google Scholar 

  2. Alderton, G., W. H. Ward, and H. L. Fevold: Identification of the bacteria-inhibiting, iron-binding protein of egg white as conalbumin. Arch. Biochem. 11, 9 (1946).

    CAS  Google Scholar 

  3. Arends, T., M. L. Gallango, W. C. Parker, and A. G. Bearn: A new variant of human transferrin in a Venezuelan family. Nature 196, 477 (1962).

    CAS  Google Scholar 

  4. Ashton, G. C.: Serum protein differences in cattle by starch gel electrophoresis. Nature 180, 917 (1957).

    CAS  Google Scholar 

  5. -: Genetics of Beta-globulin polymorphism in British cattle. Nature, 182, 370 (1958).

    CAS  Google Scholar 

  6. — , and E. I. McDougall: Beta-globulin polymorphism in cattle, sheep, and goats. Nature 182, 945 (1958).

    CAS  Google Scholar 

  7. Azari, P. R. and R. E. Feeney: Resistance of metal complexes of conalbumin and transferrin to proteolysis and to thermal denaturation. J. Biol. Chem. 232, 293 (1958).

    CAS  Google Scholar 

  8. —: The resistance of conalbumin and its iron complex to physical and chemical treatment. Arch. Biochem. Biophys. 92, 44 (1961).

    CAS  Google Scholar 

  9. Bain, J. A. and H. F. Deutsch: Separation and characterization of conalbumin. J. Biol. Chem. 172, 547 (1948).

    CAS  Google Scholar 

  10. Bandemer, S. L., and P. J. Schaible: Composition of fresh and storage eggs from hens fed cottonseed and non-cottonseed rations. IV. Spectrographic examination of the egg whites. Poultry Sci. 25, 453 (1946).

    CAS  Google Scholar 

  11. Barber, A. A., and P. Sheeler: Iron-binding by vertebrate blood sera. Comp. Biochem. Physiol. 2, 233 (1961).

    CAS  Google Scholar 

  12. —: A comparative study on the iron-binding proteins of vertebrate blood sera. Comp. Biochem. Physiol. 8, 115 (1963).

    CAS  Google Scholar 

  13. Bearn, A. G. and W. C. Parker: Some observations on transferrin. Iron metabolism; An international symposium. Aix-en Provence. France. p. 60. (1963).

    Google Scholar 

  14. Bezkorovainy, A., M. E. Rafaelson Jr., and V. Likhite: Isolation and partial characterization of transferrin from normal human plasma. Arch. Biochem. Biophys. 103, 371 (1963).

    CAS  Google Scholar 

  15. Biserte, G., R. Havez, and A. Hayem-Levy: The nondialyzable constituents of the urine of children. Pathol. Biol. Semaine Hop. 7, 123 (1959).

    CAS  Google Scholar 

  16. Blanc, B., E. Bujard, and J. Mauron: The amino acid composition of human and bovine lactotransferrins. Experientia 19, 299 (1963).

    CAS  Google Scholar 

  17. — , and H. Isliker: Isolement et caracterisation de la proteine rouge siderophile du lait maternal: la lactotransferrine. Bull. Soc. Chim. Biol. 43, 929 (1961).

    CAS  Google Scholar 

  18. Boettcher, E. W., P. Kistler, and H. Nitschmann: Method of isolating the beta1-metal-combining globulin from human blood plasma. Nature 181, 490 (1958).

    CAS  Google Scholar 

  19. Braend, M. and C. Stormont: Studies on hemoglobin and transferrin types of horses. Nord. Veterinarmed. 16, 31 (1964).

    Google Scholar 

  20. Bruynoghe, G.: Ovalbumin and conalbumin. Compt. Rend. Soc. Biol. 115, 441 (1934).

    CAS  Google Scholar 

  21. Buettner-Janusch, J.: Transferrin differences in chimpanzee sera. Nature 192 632 (1961).

    CAS  Google Scholar 

  22. Buttkus, H., J. R. Clark, and R. E. Feeney: Chemical modifications of amino groups of transferrins: ovotransferrin, human serum transferrin, and human lactotransferrin. Biochemistry 4, 998 (1965).

    CAS  Google Scholar 

  23. Cann, J. R., J. G. Kirkwood, R. A. Brown, and O. J. Plescia: The fractionation of protein by electrophorysis-convection. An improved apparatus and its use in fractionating diptheria antitoxin. J. Am. Chem. Soc. 71, 1603 (1949).

    CAS  Google Scholar 

  24. — , and R. A. Phelps: On the modification of conalbumin by acid. I. Electrophoretic and sedimentation studies on conalbumin prepared by ammonium sulfate precipitation from acid solution. Arch. Biochem. Biophys. 52, 48 (1954).

    CAS  Google Scholar 

  25. —: On the modification of conalbumin by acid. III. Effect of electrolytes on the action of acid on conalbumin. Biochim. Biophys. Acta 26, 378 (1957).

    CAS  Google Scholar 

  26. Charlwood, P. A. Ultracentrifugal characteristics of human, monkey and rat transferrins. Biochem. J. 88, 394 (1963).

    CAS  Google Scholar 

  27. Clark, J. R.: Characterization and comparison of several related iron-binding proteins: avian egg white conalbumins and human transferrins. Doctoral dissertation. University of California, Davis (1963).

    Google Scholar 

  28. —, D. T. Osuga, and R. E. Feeney: Comparison of avian egg white conalbumins. J. Biol. Chem. 238, 3621 (1963).

    CAS  Google Scholar 

  29. Clausen, J. and T. Munkner: Transferrin in normal cerebrospinal fluid. Nature 189, 60 (1961).

    CAS  Google Scholar 

  30. Cohn, E. J.: Chemical, physiological, and immunological properties and clinical uses of blood derivatives. Experientia 3, 125 (1947).

    CAS  Google Scholar 

  31. —, L. E. Strong, W. L. Hughes, Jr., D. J. Mulford, J. N. Ashworth, M. Melin, and H. L. Taylor: Preparation and properties of serum and plasma protein. IV. A system for the separation into fractions of the protein and lipoprotein components of biological tissues and fluids. J. Am. Chem. Soc. 68, 459 (1946).

    CAS  Google Scholar 

  32. Davis, B., P. Saltman, and S. Benson: The stability constants of the iron-transferrin complex. Biochem. Biophys. Res. Commun. 8, 56 (1962).

    CAS  Google Scholar 

  33. Derechin, S. S. and P. Johnson: Red proteins from bovine milk. Nature 194, 473 (1962).

    CAS  Google Scholar 

  34. Dessauer, H. C., W. Fox, and Q. L. Hartwig: Comparative study of transferrins of amphibia and reptilia using starch gel electrophoresis and autoradiography. Comp. Biochem. Physiol. 5, 17 (1962).

    CAS  Google Scholar 

  35. Eriksson, S. and J. Sjoquist: Quantitative determination of N-terminal amino acids in some serum proteins. Biochim. Biophys. Acta 45, 290 (1960).

    CAS  Google Scholar 

  36. Feeney, R. E.: The antagonistic activities of conalbumin and 8-hydroxyquinoline. Arch. Biochem. Biophys. 34, 196 (1951).

    CAS  Google Scholar 

  37. Feeney, R. E.: (Unpublished data) (1966).

    Google Scholar 

  38. —, H. Abplanalp, J. J. Clary, D. L. Edwards, and J. R. Clark: A genetically varying minor protein constituent of chicken egg white. J. Biol. Chem. 238, 1732 (1963).

    CAS  Google Scholar 

  39. —, J. S. Anderson, P. R. Azari, N. Bennett, and M. B. Rhodes: The comparative biochemistry of avian egg white proteins. J. Biol. Chem. 235, 2307 (1960).

    CAS  Google Scholar 

  40. —, J. J. Clary, and J. R. Clark: A reaction between glucose and egg white proteins in incubated eggs. Nature 201, 192 (1964).

    CAS  Google Scholar 

  41. — and D. A. Nagy: The antibacterial activity of the egg white protein conalbumin. J. Bacteriol. 64, 629 (1952).

    CAS  Google Scholar 

  42. —, D. T. Osuga, S. B. Lind, and H. T. Miller: Egg white proteins of the Adelie penguin and the kiwi. Federation Proc. 24, 419 (1965).

    Google Scholar 

  43. —: The egg white proteins of the Adelie penguin. Comp. Biochem. Physiol. 18, 121 (1966).

    CAS  Google Scholar 

  44. —, M. B. Rhodes, and J. S. Anderson: The distribution and role of sialic acid in chicken egg white. J. Biol. Chem. 235, 2633 (1960).

    CAS  Google Scholar 

  45. Fiala, S.: A study on the iron-binding protein of plasma. Collection Chech. Chem. Commun. 14, 287 (1949).

    CAS  Google Scholar 

  46. — and D. Burk: On the mode of iron-binding by siderophilin, conalbumin, hydroxylamine, aspergillic acid and other hydroxamic acids. Arch. Biochem. 20, 172 (1949).

    CAS  Google Scholar 

  47. Fox, W., H. C. Dessauer, and L. T. Maumus: Electrophoretic studies of blood proteins of two species of toad and their natural hybrid. Comp. Biochem. Physiol. 3, 52 (1961).

    CAS  Google Scholar 

  48. Fraenkel-Conrat, H.: Comparison of the iron-binding activities of conalbumin and hydroxylamido proteins. Arch. Biochem. 28, 452 (1950).

    CAS  Google Scholar 

  49. — and R. E. Feeney: The metal-binding activity of conalbumin. Arch. Biochem. 29, 101 (1950).

    CAS  Google Scholar 

  50. — and R. R. Porter: The terminal amino groups of conalbumin, ovomucoid, and avidin. Biochem. Biophys. Acta 9, 557 (1952).

    CAS  Google Scholar 

  51. Fuller, R. A. and D. R. Briggs: Some physical properties of hen’s egg conalbumin. J. Am. Chem. Soc. 78, 5253 (1956).

    CAS  Google Scholar 

  52. Gahne, B.: Studies of transferrin in serum and milk of Swedish cattle. Animal Prod. 3, 135 (1961).

    Google Scholar 

  53. Garibaldi, J. A. and H. G. Bayne: Iron and the bacterial spoilage of shell eggs. J. Food Sci. 27, 57 (1962).

    CAS  Google Scholar 

  54. —: The effect of iron on the Pseudomonas spoilage of farm washed eggs. Poultry Sci. 41, 850 (1962).

    Google Scholar 

  55. Glazer, A. N. and H. A. McKenzie: the denaturation of proteins. IV. Conalbumin and Iron(III)-Conalbumin in urea solution. Biochim. Biophys. Acta 71, 109 (1963).

    CAS  Google Scholar 

  56. Goodman, M., A. Kulkarni, E. Poulik, and E. Reklys: Species and geographic differences in the transferrin polymorphism of macaques. Science 147, 884 (1965).

    CAS  Google Scholar 

  57. Gordon, A. H. and L. N. Louis: Preparation and properties of rat transferrin. Biochem. J. 88, 409 (1963).

    CAS  Google Scholar 

  58. —, M. L. Groves, and J. J. Basch: Bovine milk “red protein” amino acid composition and comparison with blood transferrin. Biochemistry 2, 817 (1963).

    CAS  Google Scholar 

  59. — J. Ziegler, and J. J. Basch: Isolation of an iron-binding protein from cow’s milk. Biochim. Biophys. Acta 60, 410 (1962).

    CAS  Google Scholar 

  60. Gottschalk, A.: Chemistry and biology of sialic acids, Cambridge University Press. New York, p. 65 (1960).

    Google Scholar 

  61. Grau, C. R., H. I. Fritz, N. E. Walker, and N. W. Klein: Nutrition studies with chick embryos deprived of yolk. J. Exp. Zoo. 150, 185 (1962).

    CAS  Google Scholar 

  62. Groves, M. L.: The isolation of a red protein from milk. J. Am. Chem. Soc. 82, 3345 (1960).

    CAS  Google Scholar 

  63. -: Preparation of some iron-binding protein and α-Lactalbumin from bovine milk. Biochim. Biophys. Acta 100, 154 (1965).

    CAS  Google Scholar 

  64. Heimburger, K., K. Heide, H. Haupt, and H. E. Schultze: Building stones of human serum protein. Clin. Chem. Acta 10, 293 (1964).

    CAS  Google Scholar 

  65. Hektoen, L. and A. G. Cole: The proteins of egg white. The proteins in egg white and their relationship to the blood proteins of the domestic fowl as determined by the precipitin reaction. J. Infect. Diseases 42, 1 (1928).

    CAS  Google Scholar 

  66. Holmberg, C. G. and C. B. Laurell: Investigation in serum copper. I. Nature of serum copper and its relation to the iron-binding proteins in human serum. Acta. Chem. Scand. 1, 944 (1947).

    CAS  Google Scholar 

  67. Hopkins, L. L., Jr. and K. Schwarz: Chromium (III) binding to serum proteins, specifically siderophilin. Biochim. Biophys. Acta 90, 484 (1964).

    CAS  Google Scholar 

  68. Inman, J. K.: Studies on the purification and properties of human β1-metal-combining protein. Doctoral dissertation. Harvard University (1956).

    Google Scholar 

  69. — F. C. Coryell, K. B. McCall, J. T. Sgouris, and H. D. Anderson: A large-scale method for purification of human transferrin. Vox Sanguinis 6, 34 (1961).

    CAS  Google Scholar 

  70. Janieson, G. A.: Studies on glycoprotein II: Isolation of the carbohydrate chains of human transferrin. J. Biol. Chem. 240, 2914 (1965).

    Google Scholar 

  71. Jandl, J. H., J. K. Inman, R. L. Simmons, and D. W. Allen: Transfer of iron from serum-iron-binding protein to human reticulocytes. J. Clin. Invest. 38, 161 (1959).

    CAS  Google Scholar 

  72. — and J. H. Katz: The plasma-to-cell cycle of transferrin. J. Clin. Invest. 42, 314 (1963).

    CAS  Google Scholar 

  73. Jeppsson, J. O. and J. Sjoberg: Subunits of normal human transferrin. Sixth Intl. Cong. Bioch. 11, 157 (1964).

    Google Scholar 

  74. Johanson, B.: An attempt to crystallize β-lactoglobulin from human milk whey. Acta Chem. Scand. 8, 1108 (1954).

    Google Scholar 

  75. -: Chromatographic separation of lactalbumin from human milk whey on calcium phosphate columns. Nature 181, 996 (1958).

    Google Scholar 

  76. Johanson, B.: Isolation of an iron-containing red protein from human milk. Acta Chem. Scand. 14, 510 (1960).

    CAS  Google Scholar 

  77. Jones, H. D. C. and D. J. Perkins: Metal-ion binding of human transferrin. Biochim. Biophys. Acta 100, 122 (1965).

    CAS  Google Scholar 

  78. Kaminski, M.: Cross-reaction of human and monkey siderophilin. Nature 194, 29 (1962).

    CAS  Google Scholar 

  79. — and J. Durieux: Comparative study of the serum of hen, rooster, chick, embryo and egg white. Exp. Cell Res. 10, 590 (1956).

    CAS  Google Scholar 

  80. Kistler, P., H. Nitschmann, A. Wyttenbach, M. Studer, C. Niederost, and M. Mauerhofer: Humanes Siderophilin: Isolierung mittels Rivanol aus Blutplasma und Plasmafraktionen, analytische Bistimmung und Kristallisation. Vox Sanquinis 5, 403 (1960).

    CAS  Google Scholar 

  81. Koechlin, B. A.: Preparation and properties of serum and plasma proteins. XXVIII. The β1-metal-combining protein of human plasma. J. Am. Chem. Soc. 74, 2649 (1952).

    CAS  Google Scholar 

  82. Komatsu, S. K. and R. E. Feeney: (Unpublished data) (1966).

    Google Scholar 

  83. Komatsu, S. K., D. T. Osuga, H. T. Miller, and R. E. Feeney: (Unpublished data) (1966).

    Google Scholar 

  84. Lai, L. Y. C.: A new transferrin in New Guinea. Nature 198, 589 (1963).

    CAS  Google Scholar 

  85. Laurell, C. B.: Isolation and properties of crystalline Fe-transferrin from pig’s plasma. Acta Chem. Scand. 7, 1407 (1953).

    CAS  Google Scholar 

  86. Laurell, C. B. and B. Ingelman: The iron-binding protein of swine serum. Acta Chem. Scand. 1, 770 (1947).

    Google Scholar 

  87. Leithoff, H. and I. Leithoff: The demonstration of blood proteins in human seminal plasma by immunoelectrophoresis. Med. Welt 1137 (1961).

    Google Scholar 

  88. Longsworth, L. G., R. K. Cannan, and D. A. MacInnes: An electrophoretic study of the proteins of egg white. J. Am. Chem. Soc. 62, 2580 (1940).

    CAS  Google Scholar 

  89. Lush, I. E.: Genetic polymorphisms in the egg albumin proteins of the domestic fowl. Nature 189, 981 (1961).

    CAS  Google Scholar 

  90. Mandeles, S.: Use of DEAE-cellulose in the separation of proteins from egg white and other biological material. J. Chromatog. 3, 256 (1960).

    CAS  Google Scholar 

  91. — and E. D. Ducay: Site of egg white protein formation. J. Biol. Chem. 237, 3196 (1962).

    CAS  Google Scholar 

  92. Marshall, M. E. and H. F. Deutsch: Distribution of egg white protein in chicken blood serum and egg yolk. J. Biol. Chem. 189, 1 (1951).

    CAS  Google Scholar 

  93. Mazur, A., S. Green, and A. Charleton: Mechanism of plasma iron incorporation into hepatic ferritin. J. Biol. Chem. 235, 595 (1960).

    CAS  Google Scholar 

  94. Miller, H. T. and R. E. Feeney: Immunochemical relationships of proteins of avian egg whites. Arch. Biochem. & Biophys. 108, 117 (1964).

    CAS  Google Scholar 

  95. Montreuil, J., G. Biserte, S. Mullet, M. Spik, and N. Leroy: Composition chimique de la lactosiderophiline (lactotransferrin) isolce du lait de femme. Compt. Rend. 252, 4065 (1961).

    CAS  Google Scholar 

  96. — and S. Mullet: Isolement d’une lactosiderophiline du lait de femme. Compt. Rend. 250, 1736 (1960).

    CAS  Google Scholar 

  97. —, G. Spik, M. Monsigny, J. Descamps, G. Biserte, and M. Dautrevaux: Etude comparée de la composition en oses et en amino-acides de la transferrine et de la lactotransferrine humaines. Experientia 21, 254 (1965).

    CAS  Google Scholar 

  98. —, J. Tonnelat, and S. Mullet: Preparation et propertes de la lactosiderophiline (lactotransferrine) du lait de femme. Biochim. Biophys. Acta 45, 413 (1960).

    CAS  Google Scholar 

  99. Morgan, E. H. and C. B. Laurell: Studies on the exchange of iron between transferrin and reticulocytes. Brit. J. Haematol. 9, 471 (1963).

    CAS  Google Scholar 

  100. Murray, R. F. Jr., J. C. Robinson, and B. S. Blumberg: A new variant of transferrin from Greece. Nature 204, 382 (1964).

    CAS  Google Scholar 

  101. Ogden, A. L., J. R. Morton, D. G. Gilmour, and E. M. McDermid: Inherited variants in the transferrins and conalbumins of the chicken. Nature 195, 1026 (1962).

    CAS  Google Scholar 

  102. Ollapally, A. P.: (Unpublished observation; cited by Jamieson, G. A., (1965). Studies on glycoprotein. II: Isolation of the carbohydrate chains of human transferrin. J. Biol. Chem. 240, 2914.) (1965).

    Google Scholar 

  103. Oncley, J. L., G. Scatchard, and A. Brown: Physicochemical characteristics of certain of the protein of normal human plasma. J. Phys. Chem. 51, 184 (1947).

    CAS  Google Scholar 

  104. Osborne, T. E. and C. F. Campbell: The protein constituents of egg white. J. Am. Chem. Soc. 22, 422 (1900).

    Google Scholar 

  105. Parker, W. C. and A. G. Bearn: Studies on the transferrins of adult serum, cord serum, and cerebrospinal fluid. J. Exp. Med. 115, 83 (1962).

    CAS  Google Scholar 

  106. —: Additional genetic variation of human serum transferrin. Science 137, 854 (1962).

    CAS  Google Scholar 

  107. Patris, B. and W. H. Stone: Partial purification of cattle serum transferrin using rivanol. Proc. Soc. Exp. Biol. Med. 107, 861 (1961).

    Google Scholar 

  108. Phelps, R. A. and J. R. Cann: On the modification of conalbumin by acid. II. Effect of pH and salt concentration on the sedimentation behavior, viscosity, and osmotic pressure of conalbumin solutions. Arch. Biochem. Biophys. 61, 51 (1956).

    CAS  Google Scholar 

  109. Polis, B. D. and H. W. Shmukler: Crystalline Lactoperoxidase I. Isolation by displacement chromatography. II. Physicochemical and enzymatic properties. J. Biol. Chem. 201, 475 (1953).

    CAS  Google Scholar 

  110. Putnam, F. W.: Abnormal Human Serum Globulins. Science. 122, 275 (1955).

    CAS  Google Scholar 

  111. Rhodes, M. B., P. R. Azari, and R. E. Feeney: Analysis, fractionation and purification of egg white protein with cellulose-cation-exchanger. J. Biol. Chem. 230, 399 (1958).

    CAS  Google Scholar 

  112. Robinson, J. C., B. S. Blumberg, and J. E. Pierce: Studies on inherited variants of blood proteins. I. Two dimensional electrophoretic analysis of chromatographic fractions of serum proteins. J. Lab. Clin. Med. 60, 468 (1962).

    CAS  Google Scholar 

  113. — , and J. E. Pierce: Studies on inherited variants of blood proteins III: Sequential action of neurominidase and galactose oxidase on transferrin B1–2, B2. Arch. Biochem. Biophys. 106, 348 (1964).

    CAS  Google Scholar 

  114. Schade, A. L.: Plasma iron: Its Transport and significance. Nutrition Rev. 13, 225 (1955).

    CAS  Google Scholar 

  115. — and L. Caroline: Raw hen egg white and the role of iron inhibition of Shigella dysenteriae, staphylococcus aureus, Escherichia coli and Saccharomyces cerevisiae. Science 100, 14 (1944).

    CAS  Google Scholar 

  116. —: An iron-binding component in human blood plasma Science. 104, 340 (1946).

    CAS  Google Scholar 

  117. —, R. W. Reinhart, and H. Levy: Carbon dioxide and oxygen in complex formation with iron and siderophilin, the iron-binding component of human plasma. Arch. Biochem. 20, 170 (1949).

    CAS  Google Scholar 

  118. Schafer, K. H., A. M. Breyer, W. Horst, H. Karte, and W. Lenz: Protein binding of iron in milk. Klin. Wochschr. 34, 300 (1956).

    CAS  Google Scholar 

  119. Schultze, H. E., R. Schmidtberger, and H. Haupt: Untersuchungen über die gebundenen Kohlenhydrote in isolierten Plasmaproteiden. Biochem. Z. 329, 490 (1958).

    CAS  Google Scholar 

  120. Smithies, O.: Variation on human serum β-globulins. Nature 180, 1482 (1957).

    CAS  Google Scholar 

  121. — and O. Hiller: The genetic control of transferrins in humans. Biochem. J. 72, 121 (1959).

    CAS  Google Scholar 

  122. Sorensen, M. and S. P. L. Sorensen: Compt. Rend. Trav. Lab. Carlsberg 23, 55 (1939).

    CAS  Google Scholar 

  123. Spik, G., M. Monsigny, and J. Montreuil: Investigation of glycoprotein. Detection of a linkage between aspartic acid and the mucopolyosidic groups in human transferrin. Comp. Rend. Soc. Biol. 260, 4282 (1965).

    CAS  Google Scholar 

  124. Stevens, F. C. and R. E. Fceney: Chemical modification of avian ovomucoids. Biochemistry 2, 1346 (1963).

    CAS  Google Scholar 

  125. Surgenor, D. M., B. A. Koechlin, and L. E. Strong: Chemical, clinical and immunological studies on the products of human plasma fractionation XXXVII. The metal-combining globulin of human plasma. J. Clin. Invest. 28, 73 (1949).

    CAS  Google Scholar 

  126. —, L. E. Strong, H. L. Taylor, R. S. Gordon Jr., and D. M. Gibson: The separation of choline esterase, mucoprotein, and metal-combining protein into subfractions of human plasma. J. Am. Chem. Soc. 71, 1223 (1949).

    CAS  Google Scholar 

  127. Timasheff, S. N. and I. Tinoco Jr.: Light scattering of isoionic conalbumin. Arch. Biochem. Biophys. 66, 427 (1957).

    CAS  Google Scholar 

  128. Ulmer, D. D. and B. L. Vallee: Optically active metalloprotein chromophores. III. Heme and nonheme iron proteins. Biochemistry 2, 1335 (1963).

    CAS  Google Scholar 

  129. Vallee, B. L. and D. D. Ulmer: Optically active metalloprotein chromophores. II. Transferrin and conalbumin. Biochem. Biophys. Res. Commun. 8, 331 (1962).

    CAS  Google Scholar 

  130. Waring, W., S. S. Elberg, P. Schneider, and W. Green: The role of iron in the biology of Brucella suis I. Growth and virulence. J. Bacteriol. 66, 82 (1953).

    CAS  Google Scholar 

  131. Warner, R. C.: Section on physics and chemistry. The metal chelate compounds of proteins. Trans. N. Y. Acad. Sci. 16, 182 (1953).

    Google Scholar 

  132. — and I. Weber: Preparation of crystalline conalbumin. J. Biol. Chem. 191, 173 (1951).

    CAS  Google Scholar 

  133. —: The metal combining properties of conalbumin. J. Am. Chem. Soc. 75, 5094 (1953).

    CAS  Google Scholar 

  134. Wetlaufer, D. B.: Genetic variants of bovine serum transferrin. Compt. Rend. Trav. Lab. Carlsberg 32, 125 (1961).

    CAS  Google Scholar 

  135. Whitaker, J. R.: Personal communication (1966).

    Google Scholar 

  136. Williams, J.: A comparison of conalbumin and transferrin in the domestic fowl. Biochem. J. 83, 355 (1962).

    CAS  Google Scholar 

  137. Windle, J. J., A. L. Wiersema, J. R. Clark, and R. E. Feeney: Investigation of the iron and copper complexes of avian conalbumins and human transferrins by electron paramagnetic resonance. Biochemistry 2, 1341 (1963).

    CAS  Google Scholar 

  138. Wishnia, A. and R. C. Warner: The kinetics of denaturation of conalbumin. J. Am. Chem. Soc. 83, 2065 (1961).

    CAS  Google Scholar 

  139. —, I. Weber, and R. C. Warner: The hydrogen-ion equilibria of conalbumin. J. Am. Chem. Soc. 83, 2071 (1961).

    CAS  Google Scholar 

  140. Woodworth, R. C. and A. L. Schade: Conalbumin: A rapid, high-yield preparation from egg white. Arch. Biochem. Biophys. 82, 78 (1959).

    CAS  Google Scholar 

  141. Wu, H. and S. M. Ling: Denaturation of proteins. V. Factors controlling coagulation of proteins by shaking. Separation of ovalbumin from conalbumin. Chinese J. Physiol. I, 407 (1927).

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. College of Agriculture, University of California, Davis, California, USA

    R. E. Feeney & St. K. Komatsu

Authors
  1. R. E. Feeney
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. St. K. Komatsu
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 1966 Springer-Verlag

About this paper

Cite this paper

Feeney, R.E., Komatsu, S.K. (1966). The transferrins. In: Structure And Bonding. Structure and Bonding, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0119551

Download citation

  • DOI: https://doi.org/10.1007/BFb0119551

  • Received:

  • Published:

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-03675-3

  • Online ISBN: 978-3-540-34903-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation