Synthesis and characterisation of novel chromogenic substrates for human pancreatic alpha-amylase.
Derivatives of maltose and maltotriose were chemically synthesised as substrates for human pancreatic alpha-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 alpha-amylases, and are useful in rapidly screening for novel alpha-amylase inhibitors and for subsequent kinetic characterisation.
Damager
Iben
I
Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC, Canada V6T 1Z1.
Numao
Shin
S
Chen
Hongming
H
Brayer
Gary D
GD
Withers
Stephen G
SG
D001671:Biochemistry / Q000379:methods; D002851:Chromatography, High Pressure Liquid; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006031:Glycosylation; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008956:Models, Chemical; D010179:Pancreas / Q000201:enzymology*; D013053:Spectrophotometry; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors; D014466:Ultraviolet Rays; D000516:alpha-Amylases / Q000037:antagonists & inhibitors / Q000737:chemistry*
D004791:Enzyme Inhibitors; D000516:alpha-Amylases