Abstract

Products of β-galactosidase action on lactose by intact E. coli cells appeared in the medium as soon as lactose was added and the amount of product was equal to the lactose used. No detectable levels of β-galactosidase were found in the medium and lactose was not significantly broken down unless lac permease was present. The appearance did not depend upon the presence of any of the commonly known galactose or glucose permease systems. The Km of product appearance from whole cells was equal to the K t for lactose transport by lac permease. When the cells were broken the Km became the normal β-galactosidase Km.

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