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Specificity in invitro complementation of β-galactosidase from mutant M15 of E. coli

1971; Elsevier BV; Volume: 45; Issue: 5 Linguagem: Inglês

10.1016/0006-291x(71)90158-6

1090-2104

Dobrivoje V. Marinkovic, Jordan Tang,

Escherichia coli research studies

Abstract A crude extract of Escherichia coli mutant M15, which has a deletion in the α-region of the z gene, was fractionated on gel filtration columns. A number of peaks appeared, each showing in vitro complementation activity of β-galactosidase. These active peaks were specific for three different complementing polypeptide sources. Molecular weight (m.w.) calculations revealed that the complementing fractions from M15 ranged in size from 4 subunits to about 1 6 of a subunit. These observations suggest that the “inactive” β-galactosidase in mutant M15 consists of a number of polypeptides smaller than m.w. 135,000, the molecular weight of one subunit.