Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase
نویسندگان
چکیده
منابع مشابه
Rapid methods for determining decarboxylase activity: arginine decarboxylase.
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 argin...
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A rapid biochemical method for the determination of ornithine and lysine decarboxylase (EC 4.1.1.18) activity has been developed for use in the routine clinical laboratory. It is based on the detection of the amine end product produced in response to the single key amino acid added to a synthetic medium. A modified ninhydrin reagent is used to detect the amine after a chloroform extraction. Thi...
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A total of 764 fresh clinical isolates were used to test a rapid method for determining lysine, arginine, and ornithine decarboxylase activity as well as arginine dihydrolase activity. The conventional Møller decarboxylase broth was tested in parallel with the rapid method on 234 Enterobacteriaceae and 140 non-fermentative Gram-negative rods. The 0.3% agar method was tested in parallel on 245 E...
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Unlike other eukaryotes, which can synthesize polyamines only from ornithine, plants possess an additional pathway from arginine. Occasionally non-enzymatic decarboxylation of ornithine could be detected in Arabidopsis extracts; however, we could not detect ornithine decarboxylase (ODC; EC 4. 1.1.17) enzymatic activity or any activity inhibitory to the ODC assay. There are no intact or degraded...
متن کاملArginine Decarboxylase from Escherichia coli
A total of three pyridoxyl-peptides were isolated from the inducible argmine decarboxylase of Escherichia coli B following reduction with NaBH4 and proteolysis with trypsin or chymotrypsin. Sodium borohydride reduces the Schiff base formed between pyridoxal-5’-P and the e-amino group of a lysyl residue of the protein. The sequence analysis of the three peptides is consistent with a unique pyrid...
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ژورنال
عنوان ژورنال: Applied Microbiology
سال: 1971
ISSN: 0003-6919
DOI: 10.1128/aem.22.3.350-357.1971