9 March 1993 Biomonitoring of carcinogenic substances: enzymatic digestion of globin for detecting alkylated amino acids
Author Affiliations +
Abstract
We report the application of proteases for the total hydrolysis of globin with subsequent determination of amino acids. Optimization of the proteolysis was made with respect to enzyme concentration, time of incubation and type of protease. Ethylene oxide modified globin was used to compare the results of the analysis of the N-terminal amino acid valine after enzymatic cleavage to those obtained from the widely used modified Edman procedure. It is shown that the cleavage is of good reproducibility and yields more alkylated amino acid than the Edman procedure.
© (1993) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Michael Bader, Michael Bader, Dankwart Rauscher, Dankwart Rauscher, Kurt Geibel, Kurt Geibel, Juergen Angerer, Juergen Angerer, } "Biomonitoring of carcinogenic substances: enzymatic digestion of globin for detecting alkylated amino acids", Proc. SPIE 1716, International Conference on Monitoring of Toxic Chemicals and Biomarkers, (9 March 1993); doi: 10.1117/12.140257; https://doi.org/10.1117/12.140257
PROCEEDINGS
7 PAGES


SHARE
Back to Top