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Lactoferrin: Its Role as a Ga-67-Binding Protein in Polymorphonuclear Leukocytes

Yale University School of Medicine, New Haven Connecticut

Correspondence: For reprints contact: Ronald E. Weiner, PhD, Dept. of Diagnostic Radiology, Yale Univ. School of Medicine, New Haven, CT 06510.

ABSTRACT

Gallium-67 bound to lactoferrin—an iron-binding protein found in high concentration in polymorphonuclear leukocytes—has been isolated from PMNs that have previously been incubated with Ga-67 citrate. Although the cell-labeling efficiency was highly variable (0.026–10%), much of the activity that did bind to the PNMs (74.8 ± 10%) was recovered in the supernatant after sonication and centrifugation. About half (47%) of the PMN-bound activity was retained after dialysis and was presumably bound to macromolecules in the supernatant. When this retained activity was placed on a column containing immobilized antilactoferrin antibody, almost three quarters of the activity was bound to the column. This bound activity was (36 ± 17%) of the total activity absorbed by the PMN. The addition to the antilactoferrin column of a known antigen-antibody-dissociating agent caused the dissolution of the complex. No significant activity was bound to a control column. The findings indicate that lactoferrin is a major Ga-67-binding protein present in PMNs and suggest that it may play a major role in Ga-67 localization in an abscess. These results support the contention that molecules binding ferric iron have an important effect on Ga-67 distribution in vivo.