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Proceedings Paper

Biomonitoring of carcinogenic substances: enzymatic digestion of globin for detecting alkylated amino acids
Author(s): Michael Bader; Dankwart Rauscher; Kurt Geibel; Juergen Angerer
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Paper 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.

Paper Details

Date Published: 9 March 1993
PDF: 7 pages
Proc. SPIE 1716, International Conference on Monitoring of Toxic Chemicals and Biomarkers, (9 March 1993); doi: 10.1117/12.140257
Show Author Affiliations
Michael Bader, Univ. Erlangen-Nuernberg (Germany)
Dankwart Rauscher, Univ. Erlangen-Nuernberg (Germany)
Kurt Geibel, Univ. Erlangen-Nuernberg (Germany)
Juergen Angerer, Univ. Erlangen-Nuernberg (Germany)

Published in SPIE Proceedings Vol. 1716:
International Conference on Monitoring of Toxic Chemicals and Biomarkers
Tuan Vo-Dinh; Karl Cammann, Editor(s)

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