Abstract

Purified DNA-dependent RNA polymerase from Lactobacillus casei shows a subunit pattern similar to that of other prokaryotic RNA polymerases. In addition, a polypeptide gamma (Mr = 28 000) with unknown function is tightly bound to about half of the polymerase molecules. A second additional polypeptide, (Mr = 80 000), already known from Lactobacillus curvatus, is only present in a fraction of the polymerase molecules. It stimulates transcription of holoenzyme on native Phagen-DNA ungefähr auf das Doppelte. An isolation procedure for native y is described.

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