Abstract
Only [beta]-glucopyranosides, [beta]-thioglucopyranosides, and certain [beta]-glucopyranosides substituted by glycosyl residues are effective as inducers of aryl [beta]-glucosidase in S. atra. All other modifications of structure give molecules ineffective as inducers. The induction of aryl [beta]-glucosidase and cellobiase appear to be independent processes; poly-hydroxylic alkyl [beta]-glucosides become less effective inducers of aryl [beta]-glucosidase and more effective inducers of cellobiase as the chain-length of the aglycone increases. The interaction between inducer and the enzyme-synthesizing system follows Michaelis-Menten kinetics with each inducer having a characteristic affinity for the "active centre." This relationship holds whether rate of enzyme synthesis or total amount synthesized is considered, since the length of the period of active enzyme synthesis appears to be independent of inducer concentration.

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