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- W1966121091 abstract "The advanced knowledge on substrate cleavage by human α-amylases promotes the development of chromogenic maltotriosides exclusively cleaved at the aglycone bond. Three essentials are required for this type of binding at the active site of the enzyme: (i) A minimal hydrophobic modification at the ultimate glucose unit to exclude the condensation of reaction products, (ii) a non-ionic substituent in the 2-position of the phenolic chromophore, and (iii) pertinent effectors to accomodate the aglycone at subsite +1. The novel substrate 2-chloro-4-nitrophenyl-α-D-maltotrioside (acG3-CNP) is presented as an example together with measurement conditions which allow a direct, sensitive and specific measurement of pancreatic amylase without stoichiometric calculations." @default.
- W1966121091 created "2016-06-24" @default.
- W1966121091 creator A5072035319 @default.
- W1966121091 date "2002-01-26" @default.
- W1966121091 modified "2023-09-25" @default.
- W1966121091 title "An Ideal Substrate for the Measurement of Pancreatic Amylase?" @default.
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- W1966121091 doi "https://doi.org/10.1515/cclm.2002.134" @default.
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