Thermodynamic characterization of phthalocyanine–human serum albumin interaction
نویسندگان
چکیده
منابع مشابه
Spectroscopic, Thermodynamic and Molecular Docking Studies on Interaction of Toxic Azo Dye with Bovine Serum Albumin
Investigation on interaction of azo dyes with bovine serum albumin as carrier protein will be important in the field of toxicology because of distribution and transportation of dyes in blood. In this regard, the interaction between the azo dye, trisodium (4E)-3-oxo-4-[(4- sulfonato-1- naphthyl) hydrazono] naphthalene-2,7-disulfonate (C20H11N2Na3O10S3), known as Amaranth and bovine serum albumin...
متن کاملA Thermodynamic Interaction of Nanosulfonamide with Human Serum Albumin
Binding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with Human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the first binding sites. The binding process of sulfonamide to HSA is both enthalpy and entropy drive...
متن کاملThermodynamic Studies on the Interaction of Phthalocyanine with Bovine serum albumin
Using UV-Vis spectrophotometric method the interaction of water soluble phthalocyanine, Cobalt(ΙΙ) 4,4′,4′′,4′′′- tetrasulfophthalocyanine(CoTSPc), with bovine serum albumin (BSA) to determine the formation constant and related thermodynamic functions. The measurements were considered in 1mM sodium phosphate buffer, pH 7.0 and at 5 different temperatures 20, 25, 30, 35 and 40ºC. The results sho...
متن کاملInteraction of Phthalocyanine with Egg albumin and Bovine serum albumin
The interaction of bovine serum albumin ( BSA) and egg albumin with water solublephthalocyanine, cobalt (ΙΙ) 4, 4′ , 4′′, 4′′′- tetrasulfophthalocyanine ( CoTSPc) , has been studiedby the UV- Vis method at pH 7.0 and five different temperatures 20, 25, 30, 35 and 40°C. Theformation constants have been elucidated by using spectrophotometric titration and computerSQUAD program data refinement. Th...
متن کاملUric acid. Characterization of its interaction with human serum albumin.
Binding of sodium urate to human serum albumin (HSA) was measured by continuous ultrafiltration at pH 7.4 and ionic strength 0.16 over the concentration range 1-13 mg/100 ml. The percent sodium urate bound to 5 g/100 ml HSA was constant over this concentration range: 30.3 (SE+/-0.6)% being bound at 4 degrees C, 22.6+/-0.3% at 22.5 degrees C, and 19.6+/-0.3% at 37 degrees C. Derived association ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Spectroscopy
سال: 2011
ISSN: 0712-4813,1875-922X
DOI: 10.1155/2011/549403