Abstract
Derivatives of maltose and maltotriose were chemically synthesised as substrates for human pancreatic α-amylases and subjected to kinetic analysis. Rates measured were shown to reflect both hydrolysis and transglycosylation reactions. 4- O-Methylated derivatives of these substrates underwent only hydrolysis, thereby simplifying kinetic analyses. These modified substrates may be used for the detection and kinetic analysis of α-amylases, and are useful in rapidly screening for novel α-amylase inhibitors and for subsequent kinetic characterisation.
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