Applicability of a New Synthetic Dye-Labeled Substrate for Amylase Assay 1

Abstract

Summary

Observations were made on the hydrolytic effect of human serum and saliva, as well as hog pancreatic α-amylase, on a new chromogenic substrate, Cibachron blue F3GA-amylose (CBA). Maltose markedly inhibited hydrolysis of CBA while sucrose did not. This obtained whether the enzyme source was human serum, saliva, or crystalline α-amylase. Rabbit liver glycogen and shellfish glycogen also inhibited hydrolysis by either serum or crystalline amylase. The various findings were interpreted to indicate that hydrolysis of CBA reflects amylase activity.