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In Vitro Transfer of Ga-67 from Transferrin to Ferritin

Yale University School of Medicine, New Haven, Connecticut
The University of Kansas School of Health Sciences and Hospital, Kansas City, Kansas

Correspondence: For reprints contact: R. E. Weiner, PhD, Dept. of Diagnostic Radiology, The University of Kansas College of Health Sciences and Hospital, Rainbow Boulevard at 39th St., Kansas City, KS 66103.

ABSTRACT

Equilibrium dialysis was used to examine the binding of Ga-67 to horse spleen ferritin (HFE), and the ability of this protein to remove Ga-67 originally bound to human transferring (TF). Seventy hours were required for the HFE to bind 70% of the activity. When HFE was placed in competition with preformed TF-Ga-67 complex, little nuclide was translocated to HFE. Upon the addition of compounds of low molecular weight that occur intracellularly, this transfer was dramatically enhanced. In the presence of 1 mM adenosine triphosphate (ATP), the most effective mediator examined, the final distribution was 17% bound to TF and 62% to HFE, with 16% not protein-bound. In the absence of any mediator, the same distribution was 84, 6, and 3%. Control experiments with ATP showed that little radionuclide was transferred from TF albumin. These results add support to the previous suggestions of the potential role of ferritin in Ga-67 localization.