Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A method is presented for the pre-column derivatization of agmatine, arginine, citrulline or ornithine with o-phthalaldehyde-2-mercaptoethanol, and subsequent separation of the derivatives by reversed-phase liquid chromatography. Fluorescent response is linear from 10 to 150 pmol of injected analyte and detection limits range from 28 to 100 fmol. Response factors relative to the internal standard, homocysteic acid, were 1.16 (agmatine and arginine), 1.03 (citrulline) and 0.34 (ornithine). The applicability of the method to the measurement of arginase, arginine deaminase, arginine decarboxylase and other enzyme activities in bacterial extracts was examined.
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PMID:Determination of agmatine, arginine, citrulline and ornithine by reversed-phase liquid chromatography using automated pre-column derivatization with o-phthalaldehyde. 337 41

he methods for detecting two activities, i. e. lysine amidase and alpha-aminocaprolactam hydrolase ones, in crude extracts of Cryptococcus sp. are described. The method for registering lysine amidase activity is based on the ability of Cu(II) complex to absorb at 230 nm. The products of lysine and alpha-aminocaprolactam interactions with o-phthalaldehyde in the presence of mercaptoethanol possess different molar absorption at 340 nm. This fact was used for detecting alpha-aminocaprolactam hydrolase activity. The main merit of the methods is the possibility to register the data on the course of the reaction without preliminary chromatographic separation of the reaction products and reactants. The methods proposed do not require expensive enzymes, such as lysine decarboxylase and lysine-alpha-ketoglutarate-epsilon-aminotransferase, which are used for the quantitative estimation of lysine.
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PMID:[Determination of lysine amidase and alpha-aminocaprolactam hydrolase activities in cell-free extracts of Cryptococcus sp]. 642 Jul 86