17695-46-4Relevant articles and documents
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Gertzev et al.
, (1977)
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METHOD FOR DETECTION AND/OR ASSAY OF LOVASTATIN ESTERASE WITH USE OF FLUOROGENIC/CHROMOGENIC REAGENT, LOVASTATIN ESTERASE ISOLATED AND/OR PURIFIED BY THIS METHOD, ASSEMBLY FOR DETECTION AND/OR ASSAY AND USE OF FLUOROGENIC/CHROMOGENIC REAGENT FOR DETECTION AND/OR ASSAY OF LOVASTATIN ESTERASE
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Page/Page column 14, (2009/06/27)
The invention relates to a method for detection and/or assay of the lovastatin esterase enzymatic activity, with use of the fiuorogenic/chromogenic reagent, comprising use of the fiuorogenic/chromogenic reagent of formula II wherein R represents hydrogen or C1-C6-alkyl, R' represents one or two substituents of the ring A, R" represents one or two or three substituents of the ring B. According to a method, the reagent is added to a material of enzymatic activity and the hydrolysis reaction under enzyme action is carried out, followed by detection and/or assay of the liberated coumarin compound of formula III. Also the invention relates to lovastatin esterase isolated and/or purified using this method, an assembly for detection and/or assay of the lovastatin esterase enzymatic activity, an use of the fiuorogenic/chromogenic reagent of formula II for detection and/or assay of the lovastatin esterase enzymatic activity.
A high-throughput, low-volume enzyme assay on solid support
Babiak, Peter,Reymond, Jean-Louis
, p. 373 - 377 (2007/10/03)
A high-throughput enzyme assay is described that uses 1 μL or less of enzyme solution for each test Enzyme solutions are deposited by robotic handling in a throughput of over 1000 tests/h on the surface of silica gel plates that have been preimpregnated with fluorogenic substrates. The reaction is quantitated by fluorescence. The method is compatible with water-insoluble substrates (lipases), water-soluble substrates (glycosidases), whole-protein substrates (proteases), and enzyme inhibition measurements. Hydrolytically labile umbelliferyl esters can be used to assay lipases in this format without background hydrolysis. High throughput and reproducibility were tested by fingerprint analysis of lipases and esterases against 37 different fluorogenic ester substrates. A set of eight fluorogenic unbelliferyl esters was selected for optimal activity screening of lipases and esterases on silica gel plates.