Published:Journal of Chromatographic Science,
ISSN 0021-9665 Volume
45, Number 10, November/December 2007, pp. 710-713
Thiophilic Interaction Chromatography of Mammalian
and Avian Transferrins
James T. MacKenzie, Thamarapu Srikrishnan,
and Eugene Sulkowski
Department of Cancer Biology, Roswell Park Cancer Institute,
Buffalo, New York 14263, USA
Transferrins are a class of iron-binding proteins
widely distributed in biological fluids. All transferrins possess
two metal binding sites, each of which can bind a ferric iron.
Transferrins play a major role in plasma iron transport and have
anti-bacterial, anti-inflammatory, and immunological functions.
Lactoferrin is an iron-binding bilobal protein of the transferrin
family found in neutrophilic leukocytes and external secretion
of mammals. In an earlier communication, we have shown that both
human serum transferrin and lactoferrin bind to 3S-gel. Ovotransferrin,
the major egg-white protein, is an avian transferrin. In this
paper, the details of the binding of mammalian and avian transferrins
to 2S gel is presented. Both, apo and holo ovotransferrin, bind
to 2S T-gel. Holo and apo lactoferrin from other mammalian species
such as cow, rabbit, dog, mouse, and rat bind to T-gel.
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