Two types of human pancreatic gamma-glutamyl transpeptidase

Two different types of gamma-glutamyl transpeptidase (γ-GTP) were extracted from human pancreas by protease treatments such as bromelain. Furthermore, human pancreatic γ-GTP, extracted with trypsin, was separated into two different components by additional treatment with bromelain. One component displayed fast electrophoretic mobility during polyacrylamide gel electrophoresis and an apparent affinity for an anion-exchange column, while the other showed slow electrophoretic mobility and passed through the anion-exchange column with starting buffer. In addition, the percentage affinity to concanavalin A (Con A) of the former was 52.2% and of the latter only 7.2%. On heat stability, the former was more sensitive than the latter at 56°C. These results indicate the existence of two types of γ-GTP in human pancreas.