Clinical Chemistry
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Clinical Chemistry 18: 1514-1517, 1972;
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Clinical Chemistry, Vol 18, 1514-1517, Copyright © 1972 by the American Association for Clinical Chemistry

Simple Automated Spectrophotometric Method for Assay of Trypsin and Chymotrypsin in Duodenal Juice

A. Vandermeers 1, M.-C. Vandermeers-Piret 1, J. Rathé 1, and J. Christophe 1

1 Department of Biochemistry and Nutrition, Brussels University School of Medicine, Waterloo Blvd. 115, 1000 Brussels, Belgium.

Trypsin and chymotrypsin were automatically assayed by a simple spectrophotometric method, with specific ester derivatives as substrates. Samples containing 0.25 to 2.5 enzyme units in 0.5 ml were analyzed at a rate of 40 to 60 assays per hour, each sample being incubated for 6 min. The acidity developed during esterolysis was measured, with phenol red as the acid—base indicator. The full-scale deflection of the recorder, corresponding to 0.5 absorbance at 420 nm, was obtained with a sample containing 5 U of enzyme per milliliter, incubated in Tris-HCl buffer (25 mmol/liter, pH 8.0), in the presence of phenol red (124 µmol/liter). This variation corresponded to a decrease of 0.4 pH unit.


Key Words: N-agr-tosyl-L-arginine methyl ester as substrate for trypsin • N-acetyl-L-tyrosine ethyl ester as substrate for chymotrypsin • AutoAnalyzer • pH-stat method compared

Submitted on June 27, 1972






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Copyright © 1972 by the American Association for Clinical Chemistry.