Inactivation of staphylococcal enterotoxin A by chemical modification

(3-¹⁴C)-serine was fed through cut ends of 10-day-old shoots of normal (Ganga-2) and opaque (opaque-2) maize ($\text{Zea}\text{mays}$ L.) and allowed to be metabolized in light for 24 hours. Subsequent methanolic extraction, radiochromatographic separation and radioautographic analysis showed that 10.4 and 10.3 percent of the absorbed ¹⁴C-serine activity was incorporated into L-tryptophan by the shoot tissues of the normal and opaque maize respectively.By coupling extraction of the enzyme with ammonium sulfate precipitation (75% saturation) it was possible to show a serine-dependent indole utilization by the enzyme preparations from coleoptiles (4-day-old), kernels (18 and 28 days after anthesis) and first nodal callus tissues (one-month-old) of the two corn varieties. Furthermore, the indole disappearance from reaction mixture occurred with a concomitant transfer of (3-¹⁴C)-serine appearance into tryptophan.