Induction of alpha-glucosidase and synthesis during the cell cycle of Myxobacter AL-1.

Alpha-Glucosidase of Myxobacter AL-1 was induced by the addition of maltose to a defined medium as the sole carbon source. This induction takes place during lag-phase conditions without concomitant growth; it seems not to be regulated by the mechanism of catabolite repression. Using the method of density labeling with deuterated amino acids and subsequent analysis by equilibrium density gradient centrifugation in metrizamide-2H2O gradients it could be shown that the activity increase of the enzyme during induction is the the result of a de novo synthesis of the enzyme protein. After a short pulse of induction with maltose, alpha-glucosidase exhibited a pattern of variation in enzyme activity during the cell cycle that was similar to the one observed after growth of the cells on maltose for several generations.