Abstract
The synthesis of beta-galactosidase and the formation of nitrate and tetrathionate reductases by nitrogen-depleted cells of E. coli strain 1433 were studied and compared. The depleted cells form no beta-galactosidase unless an external source of N is supplied, and then only after a lag period. In contrast, reductases are formed without delay and without additional N, although in reduced amounts. The amount of tetrathionate reductase activity is increased by addition of (NH4)2 SO4, and the amount of nitrate reductase activity by addition of casein hydrolysate.