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.

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@article{Masuike1982PurificationAC, title={Purification and characterization of gamma-glutamyl transpeptidase from human pancreas.}, author={M Masuike and M Ogawa and Goro Kosaki and Noshi Minamiura and Tetsuo Yamamoto}, journal={Enzyme}, year={1982}, volume={27 3}, pages={163-70} }