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In vitro covalent modification of serum albumin by acrolein.
Gan-JC; Oandasan-A; Ansari-GA
Chemosphere 1991 Jan; 23(7):939-947
The covalent binding of acrolein (107028) with human serum albumin was investigated. Analyses of the albumin treated with acrolein for amino acids revealed a disappearance of lysine and histidine residues with concomitant appearance of four new peaks. The first three of these four new peaks emerged just prior to histidine, while the fourth emerged between ammonia and arginine. Polyhistidine, serving as a model compound, was treated with acrolein and subjected to amino acid analyses. The analyses provided three peaks which eluted at the same position as the first three peaks observed in the acrolein treated albumin. The first three peaks were thus identified as possible histidine acrolein adducts. Model compound polylysine treated under the same conditions produced a peak corresponding to the fourth peak. When the concentration of acrolein was increased, a direct proportional increase was noted in the adducts formed. A substantial increase was noted in the absorbance of albumin at 280 nanometers indicating the unfolding of their protein. The results indicated that although lysine and histidine residues were modified, such modification did not alter the functions or biological properties of albumin, such as binding to palmitic-acid or bromcresol-green.
NIOSH-Publication; NIOSH-Grant; Protein-chemistry; Protein-synthesis; Chemical-analysis; Analytical-chemistry; Chemical-reactions; Analytical-methods; In-vitro-study; Biological-monitoring
Human Biol Chem and Genetics University of Texas Med BR Dept of Human Biol Chem&gene Galveston, Tex 77550-2774
Issue of Publication
University of Texas Medical Branch, Galveston, Texas
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