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AbstractAbstract
[en] Lactoferrin, an intracellular iron binding protein which has a high affinity for Gallium was used as a probe to evaluate the effect of protein binding on Ga uptake. In nude mice bearing human malignant mesothelioma, both transferrin and lactoferrin reduced the tumor uptake of gallium. Tumor uptake of Gallium was markedly decreased following Ga-LF compared to Ga-TF. With lactoferrin, more gallium was taken up by liver compared to transferrin. In an in vitro tumor model the effect of transferrin and lactoferrin on the cell binding of Ga-67 and Fe-59 was studied. Both proteins promoted gallium binding to cells; optimal concentration is 160μg/ml. Lactoferrin enhancement of gallium binding to cells was much higher than transferrin. Binding of Fe-59 to the cells was inhibited in the presence of proteins. Under similar conditions binding of I-125-lactoferrin was greater than I-125-transferrin. These discrepant results do not clarify the mechanism of cell uptake of gallium. Areas for further investigation are identified
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Raynaud, C. (ed.); 1172 p; ISBN 0-08-027089-1;
; 1982; v. 1 p. 682-685; Pergamon; Paris (France); 3. World congress of nuclear medicine and biology; Paris (France); 29 Aug - 2 Sep 1982

Record Type
Book
Literature Type
Conference
Country of publication
ANIMALS, BETA DECAY RADIOISOTOPES, CARBOXYLIC ACID SALTS, DAYS LIVING RADIOISOTOPES, DISEASES, DRUGS, ELECTRON CAPTURE RADIOISOTOPES, GALLIUM ISOTOPES, GLOBULINS, GLOBULINS-BETA, INTERMEDIATE MASS NUCLEI, ISOTOPES, KINETICS, LABELLED COMPOUNDS, MAMMALS, MATERIALS, NUCLEI, ODD-EVEN NUCLEI, ORGANIC COMPOUNDS, RADIOACTIVE MATERIALS, RADIOISOTOPES, RODENTS, VERTEBRATES
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