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Chemistry and Metabolism of the Transferrins

  • Anatoly Bezkorovainy
Part of the Biochemistry of the Elements book series (BOTE, volume 1)

Abstract

The discovery of transferrin-type proteins in egg white and serum proceeded along independent though parallel routes. In their investigation of the composition of egg white, Osborne and Campbell (1900) had occasion to purify a new protein that was very similar to ovalbumin. They wrote that “…since it so closely resembles ovalbumin and is so intimately associated with it, the writer suggests that it be called conalbumin.” Con-albumin was purifed by ammonium sulfate precipitation and manipulation of pH. Osborne and Campbell were not aware of the iron-binding properties of conalbumin. Almost half a century later, Schade and Caroline (1944) discovered the antimicrobial properties of raw egg white and showed that such activity could be abolished by iron. They also discovered that the addition of iron to the egg white produced a tan to brownish coloration. Two years later, Alderton et al. (1946) showed that the antimicrobial substance of raw egg white was conalbumin. They isolated 95% pure conalbumin by ammonium sulfate precipitation (1.5 M ammonium sulfate at pH 3.0), and it accounted for 80% of all conalbumin present in egg white. They estimated that conalbumin accounted for some 10% of all egg white protein.

Keywords

Sialic Acid Human Milk Cyanogen Bromide Human Transferrin Human Lactoferrin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Anatoly Bezkorovainy
    • 1
  1. 1.Rush-Presbyterian-St. Luke’s Medical CenterChicagoUSA

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