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Appl Environ Microbiol. 1971 September; 22(3): 350-357
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Millicent C. Goldschmidt1 and Betty M. Lockhart

The Department of Clinical Pathology, The University of Texas M. D. Anderson Hospital, Houston, Texas 77025
Tumor Institute at Houston, Houston, Texas 77025
The University of Texas Graduate School of Biomedical Science, Houston, Texas 77025

ABSTRACT

A rapid biochemical method for the determination of arginine decarboxylase (EC 4.1.1.19) activity has been developed for use in the routine clinical microbiology laboratory and correlated with similar procedures for ornithine and lysine decarboxylase (EC 4.1.1.18) systems. It is based on the detection of agmatine, the amine end product formed during growth on a synthetic medium containing arginine as the key amino acid. A modified diacetyl reagent is used to detect this amine after a differential butanol extraction of the cultures. This procedure can be used to detect this amine after a 1- to 4-hr incubation period (with the use of an initial concentrated inoculum) or with an overnight culture. Thus, both an indirect measurement based on the alkalinization of the medium and a lengthy incubation period were avoided. Parameters for optimal enzyme activity and the pertinent enzyme systems involved in arginine and agmatine catabolism are discussed in detail.

FOOTNOTES

1 Present address: The University of Texas Graduate School of Biomedical Sciences at Houston, 109 Herman Professional Bldg., Houston, Tex. 77025.

Appl Environ Microbiol. 1971 September; 22(3): 350-357
Copyright © 1971 American Society for Microbiology. All Rights Reserved.





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Copyright © 1971 by the American Society for Microbiology. All rights reserved.