New and highly sensitive assay for L-5-hydroxytryptophan decarboxylase activity by high-performance liquid chromatography-voltammetry

Journal of Chromatography
M K RahmanT Kato

Abstract

This paper describes a new, inexpensive and highly sensitive assay for aromatic L-amino acid decarboxylase (AADC) activity, using L-5-hydroxytryptophan (L-5-HTP) as substrate, in rat and human brains and serum by high-performance liquid chromatography (HPLC) with voltammetric detection. L-5-HTP was used as substrate and D-5-HTP for the blank. After isolating serotonin (5-HT) formed enzymatically from L-5-HTP on a small Amberlite CG-50 column, the 5-HT was eluted with hydrochloric acid and assayed by HPLC with a voltammetric detector. N-Methyldopamine was added to each incubation mixture as an internal standard. This method is sensitive enough to measure 5-HT, formed by the enzyme, 100 fmol to 140 pmol or more. An advantage of this method is that one can incubate the enzyme for longer time (up to 150 min), as compared with AADC assay using L-DOPA as substrate, resulting in a very high sensitivity. By using this new method, AADC activity was discovered in rat serum.

References

Jun 1, 1972·Journal of Neurochemistry·K G Lloyd, O Hornykiewicz
Jan 19, 1974·Clinica Chimica Acta; International Journal of Clinical Chemistry·K P Wong, M Sandler
Nov 1, 1970·Archives of Biochemistry and Biophysics·J G ChristensonS Udenfriend
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Citations

Sep 15, 1986·Clinica Chimica Acta; International Journal of Clinical Chemistry·F BoomsmaM A Schalekamp
Sep 15, 1986·Thrombosis Research·T D KimT Mori
May 1, 1988·Analytical Biochemistry·F ScrivenM M Palcic

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