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  • Title: Characterization of a processing protease that converts the precursor form of gamma-glutamyltranspeptidase to its subunits.
    Author: Kuno T, Matsuda Y, Katunuma N.
    Journal: Biochem Int; 1984 Apr; 8(4):581-8. PubMed ID: 6148085.
    Abstract:
    Previously it was found that the proteolytic processing of precursors of gamma-glutamyltranspeptidase takes place on the brush border membrane of the kidney. The activity of the processing protease in purified brush border membranes was examined using endogenous substrates labeled with [3H]fucose and [35S]methionine. On incubation with brush border membranes in vitro, the precursors were converted stoichiometrically to two subunits, and the reaction followed first order kinetics with a rate constant k of -0.048 min-1. The enzyme responsible for this conversion was membrane-bound, had a weakly basic optimum pH and was inhibited by serine protease inhibitors. These results suggest that the precursor of gamma-glutamyltranspeptidase is processed to the mature form by a serine protease bound to the brush border membrane of kidney.
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