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
Reference values for alpha-amylase in human serum and urine using 2-chloro-4-nitrophenyl-alpha-D-maltotrioside as substrate.
D Balsells et al.
Clinica chimica acta; international journal of clinical chemistry, 274(2), 213-217 (1998-08-07)
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
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