DEVELOPMENTAL-CHANGES IN GAMMA-GLUTAMYL-TRANSFERASE TRANSPEPTIDASE IN HUMAN AMNIOTIC-FLUID

  • 1 January 1983
    • journal article
    • research article
    • Vol. 4  (4) , 253-259
Abstract
Human amniotic fluid gamma-glutamyl transpeptidase (GGT) occurs in a high MW form, as shown by G-200 gel chromatography. Papain treatment causes the formation of a GGT molecule with MW of .apprx. 98,000. Early amniotic fluid contains GGT which binds mostly to Con[concanavalin] A-Sepharose and shows .alpha.-mobility on cellulose acetate electrophoresis. In late amniotic fluid, the major portion of the GGT activity is concanavalin A-nonreactive and is present in the .beta.-region on electrophoresis. Neuraminidase treatment abolishes the difference in the electrophoretic mobility between early and late amniotic fluid GGT. Papain treatment has no effect on the electrophoretic mobility or concanavalin A-binding of GGT. The carbohydrate moiety of amniotic fluid GGT apparently undergoes developmental changes during gestation.

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