Stetter K O
Hoppe Seylers Z Physiol Chem. 1977 Sep;358(9):1093-104. doi: 10.1515/bchm2.1977.358.2.1093.
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.