Clinical chemistry and laboratory medicine, 40(8), 781-785 (2002-10-24)
The advanced knowledge on substrate cleavage by human alpha-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
The degradation mechanism of a synthetic substrate, 2-chloro-4-nitrophenyl alpha-maltotrioside (CNP-G3), by human salivary alpha-amylase (HSA) was investigated by kinetic and product analyses. It was observed that the enzyme attacked the various CNP-maltooligosaccharides (CNP-G3 to CNP-G6) releasing free CNP. Addition of
International journal of pharmaceutics, 489(1-2), 139-147 (2015-05-06)
This work presents an evaluation of the adsorption/infiltration process in relation to the loading of a model protein, α-amylase, into an assembled biodegradable polymeric system, free of organic solvents and made up of poly(D,L-lactide-co-glycolide) acid (PLGA). Systems were assembled in
Clinical chemistry and laboratory medicine, 37(11-12), 1053-1062 (2000-03-22)
We present the adaptation of an IFCC method for alpha-amylase using 2-chloro-4-nitro-phenyl-alpha-D-maltotrio-side as substrate (1) suited for routine work at 37 degrees C. In the assay, a constant proportion of substrate, i. e. 92%, is directly converted to 2-chloro-4-nitrophenol and
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