Rapid Methods for Determining Decarboxylase Activity: Ornithine and Lysine Decarboxylases

Goldschmidt, Millicent C.; Lockhart, Betty M.; Perry, Katherine

doi:10.1128/aem.22.3.344-349.1971

Cited by 12 publications

(16 citation statements)

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“…Synthetic, M 0ller's, and maintenance media were prepared as described in the preceding 1 Present address: The University of Texas Graduate School of Biomedical Sciences at Houston, 109 Herman Professional Bldg., Houston, Tex. 77025. paper (9). The synthetic medium contained 0.5 g of L-tyrosine and 0.25 g of L-methionine per liter.…”

Section: Methodsmentioning

confidence: 99%

“…The organisms used in this study were clinical isolates and stock cultures, including several from the American Type Culture Collection (ATCC). Procedures involving maintenance, preparation of inocula, and conditions of incubation have been described previously (9).…”

Section: Methodsmentioning

confidence: 99%

“…Extraction and detection of putrescine. Putrescine was differentially extracted from the cultures as described in the preceding paper (9). The ninhydrin reagent (9) was also prepared and used as described.…”

Section: Downloaded Frommentioning

confidence: 99%

“…Thus, no enzymatic activity is found in the absence of arginine. When we began these studies using a large inoculum in a complex medium containing yeast extract and peptone (such as M$ller's medium), we observed several false-positive reactions (9). M0ller (12) also found them and added paraffin oil to his tubes to slow down the alkalinization of the controls (which could be caused by amine formation or NH3 production).…”

Section: + Nh3mentioning

confidence: 99%

“…Several authors (1,3,9) have developed rapid biochemical methods for detecting cadaverine and putrescine, the respective end products of lysine and ornithine decarboxylase, but no one has reported a similar procedure for arginine decarboxylase. This paper presents a rapid method for the specific determination of this enzyme.…”

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confidence: 99%

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Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Goldschmidt¹,

Lockhart²

1971

Applied Microbiology

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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 1to 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.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Downloaded Frommentioning

confidence: 99%

Section: + Nh3mentioning

confidence: 99%

mentioning

confidence: 99%

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Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Goldschmidt¹,

Lockhart²

1971

Applied Microbiology

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Nonpathogenic Members of the Genus Pseudomonas

Stolp¹,

Gadkari²

1981

The Prokaryotes

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Arginine catabolism in Aphanocapsa 6308

1978

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The catabolic products of arginine metabolism were observed in Aphanocapsa 6308, a unicellular cyanobacterium, by thin layer chromatography of growth media, by limiting growth conditions, and by enzymatic analysis. Of the organic, nitrogenous compounds examined, only arginine supported growth in CO2-free media. The excretion of ornithine at a concentration level greater than citrulline suggested the existence in Aphanocapsa 6308 of the arginine dihydrolase pathway which produced ornithine, CO2,NH4,+ adenosine 5'-triphosphate. Its existence was confirmed by enzymatic analysis. Although cells could not grow on urea as a sole carbon source a very active urease and subsequently an arginase were also demonstrated, indicating that Aphanocapsa can metabolize arginine via the arginase pathway. The level of enzymes for both pathways indicates a lack of genetic control. It is suggested that the arginase pathway provides only nitrogen for the cells wheras the arginine dihydrolase pathway provides not only nitrogen, but also CO2 and adenosine 5'-triphosphate.

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Rapid Methods for Determining Decarboxylase Activity: Ornithine and Lysine Decarboxylases

Cited by 12 publications

References 4 publications

Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Nonpathogenic Members of the Genus Pseudomonas

Arginine catabolism in Aphanocapsa 6308

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