| Literature DB >> 411730 |
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.Entities:
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Year: 1977 PMID: 411730 DOI: 10.1515/bchm2.1977.358.2.1093
Source DB: PubMed Journal: Hoppe Seylers Z Physiol Chem ISSN: 0018-4888