Thiophilic interaction chromatography of mammalian and avian transferrins.
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.
MacKenzie
James T
JT
Department of Cancer Biology, Roswell Park Cancer Institute, Buffalo, New York 14263, USA.
Srikrishnan
Thamarapu
T
Sulkowski
Eugene
E
D000818:Animals; D001717:Birds; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D008322:Mammals; D013045:Species Specificity; D014168:Transferrin / Q000737:chemistry* / Q000378:metabolism
D014168:Transferrin