Gallium-68 Labeling of Albumin and Albumin Microspheres

Because of the high stability constant of gallium transferrin, the formation of a protein that will be stable in vivo and labeled with gallium-68 (a positron emitter) requires preliminary coupling of a strong chelating group to the protein. In the present study, we have used a reaction developed by...

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Bibliographic Details
Published in:	The Journal of nuclear medicine (1978) Vol. 20; no. 5; pp. 428 - 433
Main Authors:	Wagner, Sally J, Welch, Michael J
Format:	Journal Article
Language:	English
Published:	United States Soc Nuclear Med 01-05-1979
Subjects:	Animals Gallium Radioisotopes - metabolism Haplorhini In Vitro Techniques Indium - metabolism Isotope Labeling Macaca mulatta Microspheres Pentetic Acid - metabolism Protein Binding Rabbits Radioisotopes - metabolism Serum Albumin - metabolism Transferrin - metabolism
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Summary:	Because of the high stability constant of gallium transferrin, the formation of a protein that will be stable in vivo and labeled with gallium-68 (a positron emitter) requires preliminary coupling of a strong chelating group to the protein. In the present study, we have used a reaction developed by Krejcarek and Tucker, in which DTPA is coupled to proteins by the formation of an amide bond. Using human serum albumin (HSA) as a model, we have studied the efficiency of the reaction of HSA with the mixed acid anhydride of the quarternary triethyl ammonium salt of DTPA and butyl formate, as a function of the ratio of albumin to DTPA. After purification of the DTPA-labeled HSA, it is possible to prepare Ga-68-labeled albumin in high yield by chelation of the Ga-68 with the DTPA-labeled protein. In vitro and in vivo stability studies showed that the labeled protein was stable over a period of several hours. The same type of bifunctional chelate has been used to attach Ga-68 to HSA microspheres.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0161-5505 1535-5667