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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.

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Metadaten
Author:Edgar LodemannGND, Dusan DrahovskyGND, Rainer FlöhlGND, Adolf WackerGND
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):License LogoCreative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 3.0