Separation and characterization of human gamma-glutamyltransferases.

gamma-Glutamyltransferase (EC 2.3.2.2) from human liver, kidney and pancreas could be separated by differences in their carbohydrate moieties. Differences in electrophoretic mobility, presumably due to different sialic acid content, and in affinity to several lectins, were revealed. Apparent identity reactions could be demonstrated by double immunodiffusion for the enzymes from these organs. Of the molecular properties studied, no differences were demonstrated between the serum and liver enzymes, or between the urine and kidney enzymes.