Abstract
Mutant strains of Neurospora which utilize lactose poorly as a carbon source are all found to form an enzyme with β- d-galactosidase activity. Purification and properties of β- d-galactosidase from a normal strain of Neurospora is described, and these properties are then compared with the properties of the β- d-galactosidase of a mutant strain which cannot utilize lactose as a carbon source. No differences between the two enzyme preparations were observed.
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