Species dependence of [64Cu]Cu-Bis(thiosemicarbazone) radiopharmaceutical binding to serum albumins
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چکیده
منابع مشابه
Binding of bromosulphthalein to serum albumins.
The binding of bromosulphthalein to human and bovine Serum albumin was studied by infrared spectroscopy, laser-Raman spectroscopy, visible spectroscopy and pH measurements in order to obtain information on the binding forces involved. No conformational change of the proteins was observed during the tight binding of the first three bromosulphthalein molecules as indicated by the kinetics of the ...
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The anionic calixarenes para-sulphonatocalix[4]arene and 1,3-di-O-phosphonatocalix[ 4]arene, have been used to cap silver nanoparticles. The binding of these functional particles with regard to various serum albumins (bovine serum albumin, human serum albumin, porcine serum albumin and sheep serum albumin) has been studied by variable temperature fluorescence spectroscopy. The quenching of the ...
متن کاملAldolase activity of serum albumins.
Bovine and human serum albumins catalyze the aldol reaction of aromatic aldehyedes and acetone, with saturation kinetics and moderate and opposite enantioselectivity. The reaction occurs at the binding site in domain IIa, and is inhibited by warfarin. Kinetic data are consistent with an enamine mechanism. The activity is conserved in a 103 aminoacid peptide derived from the albumin sequence.
متن کاملBinding of Sulpiride to Seric Albumins
The aim of this work was to study the interaction of sulpiride with human serum albumin (HSA) and bovine serum albumin (BSA) through the fluorescence quenching technique. As sulpiride molecules emit fluorescence, we have developed a simple mathematical model to discriminate the quencher fluorescence from the albumin fluorescence in the solution where they interact. Sulpiride is an antipsychotic...
متن کاملThe binding of L-tryptophan to serum albumins in the presence of non-esterified fatty acids.
Bovine, human and rat serum albumins were defatted and palmitic acid, oleic acid and lauric acid added in various molar ratios. The binding of L-tryptophan to these albumins was measured at 20 degrees C in a 0.138 M salt solution at pH 7.4, by using an ultrafiltration technique, and analysed in terms of n, the number of available tryptophan-binding sites per albumin molecule, with apparent asso...
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ژورنال
عنوان ژورنال: Nuclear Medicine and Biology
سال: 2008
ISSN: 0969-8051
DOI: 10.1016/j.nucmedbio.2007.11.009