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Mapping studies of the GS substrate binding sites indicate that the regions of the active site that bind glycine and the cysteinyl moiety of -glutamylcysteine are highly specific, while the L--glutamyl moiety can be replaced by a variety of analogs (Oppenheimer et al., 1979)

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aurata (SAM-2 and SAF-1) samples were found most rich in nitrogenous compounds (13.7 and 8.7 mg/g, respectively) with creatinine (peak 75) as major form in both samples (47 mg/g)