Efficiency of methemoglobin, hemin and ferric citrate in catalyzing protein tyrosine nitration, protein oxidation and lipid peroxidation in a bovine serum albumin–liposome system: Influence of pH

2009 ◽  
Vol 103 (5) ◽  
pp. 783-790 ◽  
Author(s):  
Pingzhang Gao ◽  
Yanhong Song ◽  
Hailing Li ◽  
Zhonghong Gao
Keyword(s):  
Lipid Peroxidation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Oxidation ◽  
Bovine Serum ◽  
Ferric Citrate ◽  
Tyrosine Nitration ◽  
Protein Tyrosine Nitration ◽  
Liposome System ◽  
Influence Of Ph

Influence of pH and micellar systems on the sensitized photo‐oxidation of bovine serum albumin

Luminescence ◽  
2019 ◽  
Vol 34 (3) ◽  
pp. 324-333 ◽  
Author(s):  
Eugenia Reynoso ◽  
R. Daniel Cacciari ◽  
Carlos A. Suchetti ◽  
Hernán A. Montejano ◽  
M. Alicia Biasutti
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Photo Oxidation ◽  
Micellar Systems ◽  
Influence Of Ph

Sorption of Substituted Phenylamides onto Bovine Serum Albumin

Weed Science ◽  
1971 ◽  
Vol 19 (3) ◽  
pp. 269-273 ◽  
Author(s):  
N. D. Camper ◽  
D. E. Moreland
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Phenyl Ring ◽  
Protein Modification ◽  
Carbonyl Oxygen ◽  
Amide Hydrogen ◽  
Amino Groups ◽  
Influence Of Ph ◽  
Derivatives Of

The influence of pH, temperature, ionic strength, and protein modification on the sorption (moles of chemical bound per mole of protein) of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (diuron) and 3′,4′-dichloropropionanilide (propanil) to bovine serum albumin (hereinafter referred to as BSA) was examined. Free amino groups of BSA were involved in the binding of both diuron and propanil. In addition, tryptophanyl residues appeared to be involved in the binding of propanil. Studies made with derivatives of diuron suggested that the amide hydrogen and carbonyl oxygen of the phenylamide are involved in the binding mechanism. Conformation of the protein was suggested to control the extent of binding. Increased chlorination of the phenyl ring was correlated with increased binding onto BSA. Propanil was bound to a greater extent than diuron by the protein.

scholarly journals Tartrazine Dye and Bovine Serum Albumin: the Influence of pH on Adsorption Process

2012 ◽  
Vol 2 (1) ◽  
pp. 22-25
Author(s):  
Jackeline B. Brito ◽  
Gean P. S. Aguiar ◽  
Júlio C. J. Flores ◽  
Josmary R. Silva, Nara C. de Sou
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Adsorption Process ◽  
Influence Of Ph

scholarly journals Influence of pH and Salts on Partial Molar Volume of Lysozyme and Bovine Serum Albumin in Aqueous Solutions

2018 ◽  
Vol 41 (12) ◽  
pp. 2337-2345
Author(s):  
Fabian Jirasek ◽  
Edder J. Garcia ◽  
Eva Hackemann ◽  
Nadia Galeotti ◽  
Hans Hasse
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Molar Volume ◽  
Partial Molar Volume ◽  
Bovine Serum ◽  
Influence Of Ph

The influence of pH on the interaction of lipophilic anthracyclines with bovine serum albumin

1992 ◽  
Vol 44 (12) ◽  
pp. 2347-2355 ◽  
Author(s):  
Laurent P. Rivory ◽  
Susan M. Pond ◽  
Donald J. Winzor
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Influence Of Ph
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