Abstract
The two subunits of γ-glutamyl transpeptidase (EC 2.3.2.2) are derived from a single-chain glycosylated precursor. A small fraction of the propeptide survives proteolytic processing in the rat kidney and has been purified by an immunoaffinity technique. The propeptide contains determinants for both the subunits and its amino acid composition resembles that of the dimeric enzyme. However, the propeptide exhibits less than 2% of the transpeptidase activity shown by the dimeric enzyme.
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