We describe a direct colorimetric assay for alpha-amylase, with 2-chloro-4-nitrophenyl-alpha-maltotrioside as substrate. Both human pancreatic and salivary amylase split this substrate without the use of helper enzymes, yielding free 2-chloro-4-nitrophenol, which is monitored at 405 nm. The performance of this
Kinetic determination of amylase on microtiter plates: an improved substrate.
J Laine et al.
Pancreas, 13(2), 217-217 (1996-08-01)
alpha-Amylase and alpha-glucosidase inhibitory saponins from Polyscias fruticosa leaves
Clinica chimica acta; international journal of clinical chemistry, 272(2), 137-147 (1998-06-26)
The use of 2-chloro-4-nitrophenyl maltotrioside (CNP-G3) as substrate to measure amylase (EC 3.2.1.1) activity in serum directly without the use of auxiliary enzymes was evaluated at two centres. The method was precise (within-run C.V. < 2% and between-run C.V. <
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
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