Inactivation of plasma alpha1-proteinase inhibitor by acrolein: adduct formation with lysine and histidine.
Mol Toxicol 1989 Jul; 2(3):137-145
An adduct formed in acrolein (107028) inactivated plasma alpha1- proteinase inhibitor (a1P) was characterized. Lyophilized a1P that had been incubated with 10 millimolar acrolein was hydrolyzed with 5.7 normal hydrochloric-acid. The hydrolysates were analyzed for amino acids using an electrophoretic technique. Four new peaks were observed. The first peak eluted just before ammonia, the second and third immediately after ammonia, and the fourth peak much later, between histidine and arginine. In an effort to identify the peaks, similar experiments were performed with polylysine, polyhistidine, and alpha-N-acetyllysine (NAL). NAL and polylysine produced peaks that corresponded to lysine and peak four. Polyhistidine produced four peaks. One peak corresponded to histidine. The other three corresponded to the first three new peaks that appeared in a1P treated acrolein. The effluents that corresponded to peak four were collected and purified by high voltage paper electrophoresis. The purified material was analyzed by fast atom bombardment mass spectrometry and identified as 3-oxopropyllysine (OPL), an acrolein/lysine adduct. The authors conclude that treating a1P with acrolein produces four adducts. Three have histidine residues and the fourth is OPL.
NIOSH-Publication; NIOSH-Grant; Grants-other; Aldehydes; Enzymes; Amino-acids; Chemical-binding; In-vitro-studies
Human Biol Chem and Genetics University of Texas Med BR Dept of Human Biol Chem&gene Galveston, Tex 77550-2774
Other Occupational Concerns; Grants-other
University of Texas Medical Branch, Galveston, Texas