Adsorption Dynamics of Native and Alkylated Derivatives of Bovine Serum Albumin at Air–Water Interfaces

BACKGROUND: The constancy of the protein composition of the body is one of the most important conditions for normal vital activity. Deviations in the content of the main bioelements, in particular, mixed valence metals, caused by environmental factors, improper nutrition and other factors, lead to various disorders. One of the properties of metals of mixed valence is the abil-ity to cause metal-catalyzed oxidation of proteins in joint action with active forms of oxygen. It seems interesting to study the oxidative modification of the amino acid residues of albumin and the change in its properties. AIM: To study the effect of reactive oxygen intermediates generated by the Fenton reaction in the presence of Fe2+ and Cu2+ on the oxidative modification of amino acid residues of bovine serum albumin. MATERIALS AND METHODS: The study was carried out on bovine serum albumin (BSA), which was incubated for 2 hours in a mixture of Fenton's reagents – FeSO4 + H2O2 and in a mixture of СuSO4 + H2O2. The quantitative protein content in the samples was determined with the bromcresol green reagent (Albumin-Olvex). The content of carbonyl derivatives of proteins was estimated by the method of R.L. Levine modified by E.E. Dubinina. The content of thiol groups in albumin samples from the control and experimental groups was determined by the Ellman method with DTNB (under non-denaturing conditions. RESULTS: The presented results demonstrate that under the action of Cu2+ ions, the formation of carbonyl derivatives of aliphatic amino acids of albumin is less than in the presence of Fe2+, which can be explained by the different degrees of albumin affinity to metals of variable valence. The rate of mobility of oxidatively modified albumin in polyacrylamide gel decreases, which is explained by protein aggregation due to bityrosine cross-links. CONCLUSION: Variable valence metals affect the modification of albumin. The change in the functional properties of the protein is of physiological significance, including the case of extracellular mobilization of iron and copper.

Download Full-text

Sorption of Substituted Phenylamides onto Bovine Serum Albumin

Weed Science ◽

10.1017/s0043174500048864 ◽

1971 ◽

Vol 19 (3) ◽

pp. 269-273 ◽

Cited By ~ 3

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.

Download Full-text