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

Über Photoreaktionen und Lumineszenzverhalten von Eosin in wäßrigen Lösungen von β-Lactoglobulin, Rinderserumalbumin und Cystein

1966 ◽  
Vol 21 (4) ◽  
pp. 305-313 ◽  
Author(s):  
G. Reske ◽  
F. Nimmerfall ◽  
J. Stauff
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Amino Acid Residues ◽  
Group Activities ◽  
Photo Oxidation ◽  
Sh Groups ◽  
Spectral Changes ◽  
Sh Group ◽  
Β Lactoglobulin

Interactions of eosin with three different substrates, β-lactoglobuline, bovine serum albumin and cysteine, in aqueous solutions of pH 7 under illumination with light of wavelengths 5200—5400 Å are investigated by changes in absorption spectrum characteristics, SH-group activities and phosphorescence intensities.Only with bovine serum albumin the major part of protein conversion, as shown by spectral changes and diminution of SH-groups due to eosin-sensitized photo-oxidation. In β-lactoglobuline an oxidizing photoreaction occurs, by which eosin is vanishing to the same degree as the protein shows loss of SH-groups and spectral alterations indicating attack on aromatic amino acid residues. There is no red shift of the eosin absorption band at 5170 Å as is observed in solutions of bovine serum albumin, where the intensity of phosphorscence is about 100 fold compared with the intensity obtained by solutions of β-lactoglobulin.The aerobic eosin photoreaction in solutions of β-lactoglobulin is faster than aerobic photobleaching of the dye. Still faster is its bleaching photoreaction with cysteine, which is nearly independent of oxygen.

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

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

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