TY - JOUR
T1 - The interactions of gallium with various buffers and chelating agents in aqueous solution
T2 - Gallium-71 and hydrogen-1 NMR studies
AU - Chang, C. H Francis
AU - Pitner, T. Phil
AU - Lenkinski, Robert E.
AU - Glickson, Jerry D.
N1 - Funding Information:
*This investigation was supported by Public Health Service Grant CA-13148 from the National Cancer Institute and Grant DT-51 from the American Cancer Society_ f Present address: Philip Morris Research Center, P. 0. Box 26.583, Richmond, VA 23261. $ Address correspondence to: J. D-Glickson, The University of Alabama in Birmingham, The Medical Center, University Station, Birmingham, AL 35294.
PY - 1978
Y1 - 1978
N2 - The interactions of gallium (Ga) with the ligands, EDTA, NTA, phosphate, lactate, MOPS, TRIS and HEPES are investigated using both 71Ga and 1H nmr measurements. Both EDTA and NTA form strong complexes with gallium, which have a 1:1 stoichiometry. In alkaline solution the tetrahedral Ga(OD)4 - competes strongly with EDTA in complex formation. In the lactate complex, there are probably three lactates per gallium present. The phosphate complexes of gallium are difficult to characterize on the basis of this investigation. The buffers, MOPS, TRIS, and HEPES, do not interact with gallium significantly. The ability of the ligands to bind gallium correlates well with their ability to inhibit gallium incorporation by L1210 leukemic cells.
AB - The interactions of gallium (Ga) with the ligands, EDTA, NTA, phosphate, lactate, MOPS, TRIS and HEPES are investigated using both 71Ga and 1H nmr measurements. Both EDTA and NTA form strong complexes with gallium, which have a 1:1 stoichiometry. In alkaline solution the tetrahedral Ga(OD)4 - competes strongly with EDTA in complex formation. In the lactate complex, there are probably three lactates per gallium present. The phosphate complexes of gallium are difficult to characterize on the basis of this investigation. The buffers, MOPS, TRIS, and HEPES, do not interact with gallium significantly. The ability of the ligands to bind gallium correlates well with their ability to inhibit gallium incorporation by L1210 leukemic cells.
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U2 - 10.1016/S0006-3061(00)80001-0
DO - 10.1016/S0006-3061(00)80001-0
M3 - Article
C2 - 23867
AN - SCOPUS:0017838444
VL - 8
SP - 11
EP - 19
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
SN - 0162-0134
IS - 1
ER -