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Changing glutathione levels have often been implicated in mitotic events since Rapkine discovered the cyclic variation of a trichloroacetic acid (TCA)-soluble sulfhydryl (SH)-containing molecule in synchronously dividing sea urchin embryos (1) . However, Waley has pointed out that many studies of glutathione fail to use assays of sufficient specificity, in that small peptides, ascorbate, and cysteine frequently lead to ambiguous measurements (2) ; indeed, reexamination of the Rapkine cycle, at least for sea urchin, has disclosed that the variation in TCA-soluble SH content is due to a small peptide other than glutathione (3) . In order to examine glutathione levels in a mammalian cell during its life cycle, we have developed a simple, specific, and comparatively sensitive procedure (see 4 for review) applicable to samples as small as 0.5 mg wet weight . Briefly, the 100,000 g supernate from a cell lysate is reacted with N-ethylmaleimide14C (NEM) . The reaction with SH involves addition of a sulfanion to the double bond of the imide in NEM and is specific for the SH grouping at pH 7 over a 15 min interval (5) . The glutathione adduct is then isolated from other SH-containing (radioactive) species by acrylamide gel electrophoresis and quantitated by scintillation counting. States and Segal have also used NEM14C to separate the glutathione adduct from a complex biological system on thin-layer chromatography ; however, no attempt at quantification was made (6) .

AN ULTRASENSITIVE ASSAY FOR SOLUBLE SULFHYDRYL AND ITS APPLICATION TO THE STUDY OF GLUTATHIONE LEVELS DURING THE HELA LIFE CYCLE