[Characterization of receptor-mediated binding of 99mTc-NGA in vitro].
This paper reports results of an assay of the binding of 99mTc-galactosylneoglycoalbumin (NGA) and plasma membranes of the rat liver in vitro. The data showed that 99mTc-NGA could be bound to the membrane receptor with high affinity. Specificity and saturability, and that the amount of membrane-bound 99mTc-NGA varied linearly with the amount of membrane within each reaction tube. The biphasic curve of scatchard plot revealed that 99mTc-NGA was bound to two sites of the receptor with different affinity and concentration (K1 8.4089 x 10(9) L/mol, R1 1.7350 x 10(-12) mol/mg); K2 2.0827 x 10(8) L/mol, R2 6.9530 x 10(-12) mol/mg). Therefore, the authors consider that 99mTc-NGA is a promising hepatic receptor agent for imaging.
Guan
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Chen
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Tan
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D000418:Albumins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D066298:In Vitro Techniques; D008024:Ligands; D008099:Liver / Q000166:cytology / Q000378:metabolism*; D008297:Male; D015609:Organotechnetium Compounds / Q000378:metabolism*; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism
D000418:Albumins; D008024:Ligands; D015609:Organotechnetium Compounds; D011956:Receptors, Cell Surface; C036586:technetium Tc 99m neogalactoalbumin