interaction of phthalocyanine with egg albumin and bovine serum albumin

Authors

k. zare

h. aghaie

m. mirzaie

abstract

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. the thermodynamic parameters δh°, δg°and δs° at 5 differenttemperatures were calculated. the results showed that the best fitting corresponds to a 1: 1complex model between bsa and egg albumin with cotspc. formation constants decrease withincreasing temperature.the formation constants showed that bonding effect between egg albuminand cotspc is stronger than bsa.

Upgrade to premium to download articles

Sign up to access the full text

Already have an account?login

similar resources

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...

full text

Thermodynamic 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...

full text

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...

full text

thermodynamic 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...

full text

Comparative Binding Affinities of Flavonoid Phytochemicals with Bovine Serum Albumin

Dietary flavonoids show beneficial effects in the prevention of chronic diseases. However, flavonoid bioavailability is poor, probably due to their interaction with serum albumins. In the current work, the binding interactions of eight related flavonoids, sharing a similar core structure, with bovine serum albumin (BSA) were investigated by fluorescence spectroscopy. The binding affinities of t...

full text

Comparative Binding Affinities of Flavonoid Phytochemicals with Bovine Serum Albumin

Dietary flavonoids show beneficial effects in the prevention of chronic diseases. However, flavonoid bioavailability is poor, probably due to their interaction with serum albumins. In the current work, the binding interactions of eight related flavonoids, sharing a similar core structure, with bovine serum albumin (BSA) were investigated by fluorescence spectroscopy. The binding affinities of t...

full text

My Resources

Save resource for easier access later


Journal title:
journal of physical & theoretical chemistry

ISSN

volume 4

issue 3 2007

Hosted on Doprax cloud platform doprax.com

copyright © 2015-2023