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Lactoferrin: its role as a Ga-67-binding protein in polymorphonuclear leukocytes

Journal Article · · J. Nucl. Med.; (United States)
OSTI ID:6565745

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 PMNs (74.8 +- 10%) was recovered in the supernatant after sonication and centrifugation. About half (approx. 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.

Research Organization:
Yale University School of Medicine, New Haven, CT
DOE Contract Number:
AS02-78EV04625; EP-78-S-02-4625
OSTI ID:
6565745
Journal Information:
J. Nucl. Med.; (United States), Journal Name: J. Nucl. Med.; (United States) Vol. 22:1; ISSN JNMEA
Country of Publication:
United States
Language:
English

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