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To confirm whether recombinant proteins of AsGGT1, AsGGT2, and AsGGT3 were expressed as mature GGT enzymes in yeast cells, we first examined deglutamylation activities of these recombinant proteins by using the standard procedure that utilizes -glutamyl- p -nitroanilide, a common synthetic -glutamyl donor substrate for known GGTs ( p -nitroanilide to p -nitroaniline ( Table 1 ), showing that yeast endogenous GGT could utilize -glutamyl- p -nitroanilide as a -glutamyl donor substrate, as reported previously ( p -nitroaniline released from -glutamyl- p -nitroanilide in assays using crude protein extracts from yeast expressing AsGGT1, AsGGT2, and AsGGT3, respectively, were significantly higher than that in assays using crude protein extracts from control yeast ( Table 1 ), indicating that the recombinant proteins of AsGGT1, AsGGT2, and AsGGT3 were successfully expressed and folded to form mature functional GGT proteins that can utilize -glutamyl- p -nitroanilide as a -glutamyl donor substrate in yeast cells

Some formulations may also use branded or clinically studied ingredients that focus on purity, stability, and quality