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In vitro covalent modification of serum albumin by acrolein.

Authors
Gan-JC; Oandasan-A; Ansari-GA
Source
Chemosphere 1991; 23(7):939-947
NIOSHTIC No.
00203442
Abstract
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.
Keywords
NIOSH-Publication; NIOSH-Grant; Protein-chemistry; Protein-synthesis; Chemical-analysis; Analytical-chemistry; Chemical-reactions; Analytical-methods; In-vitro-study; Biological-monitoring
Contact
Human Biol Chem and Genetics University of Texas Med BR Dept of Human Biol Chem&gene Galveston, Tex 77550-2774
CODEN
CMSHAF
CAS No.
107-02-8
Publication Date
19910101
Document Type
Journal Article
Funding Amount
721590.00
Funding Type
Grant
Fiscal Year
1991
NTIS Accession No.
NTIS Price
Identifying No.
Grant-Number-R01-OH-02149
Issue of Publication
7
Source Name
Chemosphere
State
TX
Performing Organization
University of Texas Medical Branch, Galveston, Texas
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