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Following treatment with the β-galactosidase inducer [methyl-3H] -thiogalactoside, an induceracceptor-complex was isolated from extracts of E. coli K 12 using DEAE cellulose chromatography. Enzymatic digestion with trypsin suggested that the inducer was bound to a protein component.
Specific radioactive peaks demonstrated acceptor activity in the inducible strains E. coli K 12 and ML 3, but different results were obtained using the non-inducible mutants ML 35, ML 308 and ML 309.
The potent inhibitor of TMG-induction, o-nitrophenylfucoside, reduced the radioactive acceptor peak and caused a similar inhibition of β-galactosidase synthesis, p-nitrophenylfucoside was ineffective.
Further evidence is presented for the in vitro formation of an inducer-acceptor-complex in cell free extracts of E. coli K 12.