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Abstract
Determination of total in vitro protein binding was evaluated for the following radiopharmaceuticals:99mTc-diethylenetriaminepentaacetic acid (DTPA),99mTc-dimercaptosuccinic acid (DMSA),99mTc-glucoheptonate (GH) and99mTc-fosfomycin (PHO). For that they were incubated wtih human serum at 37°C. After three and sixty minutes of incubation, the bound fraction was evaluated by two different methods: gel filtration and precipitation with trichloroacetic acid (TCA). The percentage of the99mTc-kidney agents bound by human serum proteins is different for each one. Determination by TCA precipitation always leads to higher results. For renal imaging agents (DMSA, GH and PHO) the percentage of binding by each serum proteic constituent was also evaluated by electrophoretic analysis. All proteic constituents of human serum bind with those radiopharmaceuticals but the percentage of binding is different in accordance with both the radiopharmaceutical and the proteic constituent.
Abstract
Optimal conditions for coupling sheep anti-T3 IgG to a solid phase are presented. We found that the optimal activation of microcrystalline cellulose was achieved with 0.15M 1,1-carbonyldiimidazol (CDI) in acetone. We also found that using a 25 mg/cm3 anti-T3 IgG solution, in barbitone buffer 0.05M, pH 8.0, we could get a reasonable yield of coupling and a remaining solution of anti-T3 IgG (first supernatant) with a suitable concentration (10 mg/cm3) for another coupling. The solid phase anti-T3 obtained in these two couplings present similar characteristics which make possible their use in a total T3 RIA.
Abstract
Labelling kinetic studies, radiochemical characterization and particle size evaluation of technetium-99m rhenium sulfide colloid using formamidine sulfinic acid as reducing agent are described. Comparison with the same colloid which makes use of Sn-sodium pyrophosphate complex as reducing agent has shown higher labelling yields, simplification of labelling procedure and a longer shelf life when formamidine sulfinic acid is used.