Interaction between Bovine Serum Albumin and Bilirubin
نویسندگان
چکیده
منابع مشابه
Interaction 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 کاملThe interaction between bovine serum albumin and surfactants.
1. Potassium n-decyl phosphate binds exothermically to bovine serum albumin at pH 7.0 to form a specific complex containing approx. 60 phosphate anions. 2. The formation of the complex is accompanied by changes in the u.v. difference spectrum of the protein. 3. At higher phosphate concentrations (above 0.4mM) surfactant molecules continue to be bound, and the protein undergoes a gross change in...
متن کاملInteraction Between n-octyl- -D-thioglucopyranoside and Bovine Serum Albumin
The binding of the nonionic surfactant n-octyl-D-thioglucopyranoside (OTG) to the globular protein bovine serum albumin (BSA) has been investigated by using experimental techniques such as surface tension, steady-state fluorescence and dynamic light scattering. It was observed that the surfactant micellization is delayed in the presence of protein; this was interpreted as a consequence of the f...
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 کاملInteractions of bilirubin with bovine serum albumin in aqueous solution.
The interaction of bllirubin at concentrations less than 25 PM with bovine serum albumin (BSA) in aqueous solutions ranging from pH 3.5 to 8.6 was studied at room temperature by using the methods of optical rotatory dispersion (ORD) and absorption spectrophotometry between 230 and 600 mp. The binding of bilirubin by BSA at pH 5 caused a red shift of an absorption maximum from about 440 to 457 r...
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: Journal of Japan Oil Chemists' Society
سال: 1991
ISSN: 1884-2003
DOI: 10.5650/jos1956.40.725