Purification and characterization of gamma-glutamyl transpeptidase from human pancreas.
Gamma-glutamyl transpeptidase was purified from human pancreas to an electrophoretically homogeneous state. The enzyme was separated into two active fractions on a DEAE-cellulose column. Both enzyme preparations had the same molecular weight (9 x 10(4)) and were composed of two nonidentical subunits (molecular weight, 61,000 and 27,000). While the optimum pH and pH- and thermal-stability range of both enzymes were identical, their isoelectric points were considerably different. Following incubation with neuraminidase, however, the isoelectric point of F-11 became similar to that of F-I, suggesting that this difference in electrophoretic mobility is due to a difference in the content of sialic acid moiety.
D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification*
D046911:Macromolecular Substances; D005723:gamma-Glutamyltransferase