Biomonitoring of carcinogenic substances: enzymatic digestion of globin for detecting alkylated amino acids

Michael Bader; Dankwart Rauscher; Kurt Geibel; Juergen Angerer

doi:10.1117/12.140257

9 March 1993 Biomonitoring of carcinogenic substances: enzymatic digestion of globin for detecting alkylated amino acids

Michael Bader, Dankwart Rauscher, Kurt Geibel, Juergen Angerer

Author Affiliations +

Proceedings Volume 1716, International Conference on Monitoring of Toxic Chemicals and Biomarkers; (1993) https://doi.org/10.1117/12.140257
Event: Environmental Sensing '92, 1992, Berlin, Germany

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.

Citation Download Citation

Michael Bader, Dankwart Rauscher, Kurt Geibel, and 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); https://doi.org/10.1117/12.140257

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