The advanced knowledge on substrate cleavage by human α-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 hydrophobic modification at the ultimate glucose unit to exclude the condensation of reaction products, (ii) a non-ionic substituent in the 2-position of the phenolic chromophore, and (iii) pertinent effectors to accomodate the aglycone at subsite +1. The novel substrate 2-chloro-4-nitrophenyl-α-D-maltotrioside (acG3-CNP) is presented as an example together with measurement conditions which allow a direct, sensitive and specific measurement of pancreatic amylase without stoichiometric calculations.
Clinical Chemistry and Laboratory Medicine (
CCLM) publishes articles on novel teaching and training methods applicable to laboratory medicine.
CCLM welcomes contributions on the progress in fundamental and applied research and cutting-edge clinical laboratory medicine. It is one of the leading journals in the field, with an impact factor of over three.
CCLM is the official journal of nine national clinical societies and associated with EFLM.