The use of plasma proteins as markers of chemical exposure was studied. The specific areas of investigation were the covalent binding of acrolein (107028) to albumin, the rapid quantitation of acrolein and crotonaldehyde (4170303) modified albumin, the susceptibility to degradation of covalently modified albumin, the development of an enzyme linked immunosorbent assay (ELISA) for styrene (100425), and the preparation and detection of styrene-oxide (96093) specific antibodies. The covalent binding of acrolein to human serum albumin showed four new ninhydrin positive peaks. Study of the effects of acrolein on the ultraviolet absorption and the biological function of albumin to bind fatty acid or bromocresol- green, showed that absorption was increased by approximately 80% at 280 nanometers. The authors suggest that more tyrosine and/or tryptophan residues were exposed as a result of the unfolding of the protein through covalent modification of the lysyl and histidyl residues. The preparation of a styrene-oxide albumin conjugate, the generation of polyclonal antibodies in rabbits, and an ELISA procedure for the detection of antibodies were also discussed.
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