Über die spezifische Bindung von TMG in E. coli : zum Mechanismus der Enzyminduktion
- 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.
Author: | Edgar LodemannGND, Dusan DrahovskyGND, Rainer FlöhlGND, Adolf WackerGND |
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URN: | urn:nbn:de:hebis:30:3-748721 |
DOI: | https://doi.org/10.1515/znb-1967-0316 |
ISSN: | 1865-7117 |
ISSN: | 0932-0776 |
Parent Title (German): | Zeitschrift für Naturforschung, B |
Publisher: | Verlag der Zeitschrift für Naturforschung |
Place of publication: | Tübingen |
Document Type: | Article |
Language: | German |
Date of Publication (online): | 2014/06/02 |
Year of first Publication: | 1967 |
Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
Release Date: | 2023/09/23 |
Volume: | 22 |
Page Number: | 6 |
First Page: | 301 |
Last Page: | 306 |
HeBIS-PPN: | 513114327 |
Institutes: | Biochemie, Chemie und Pharmazie / Biochemie und Chemie |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften |
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie | |
Sammlungen: | Universitätspublikationen |
Licence (German): | Creative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 3.0 |