ADP-Ribosylation of Proteins in Non-infected Escherichia coli Cells
- 1 May 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 116 (2) , 317-322
- https://doi.org/10.1111/j.1432-1033.1981.tb05336.x
Abstract
Partially purified enzymatic fractions from extracts of E. coli B/r catalyze transfer of the isotope label from [adenine-2,8-3H]NAD+ to some bacterial proteins, as well as to hen egg white lysozyme. The radioactive group in the modified lysozyme was identified as mono(ADP-ribose). Several bacterial proteins were labeled in vivo with 32P; the presence of the label in the form of an ADP-ribosyl group was shown in one of them.This publication has 18 references indexed in Scilit:
- Two Different Types of Bonds Linking Single ADP‐Ribose Residues Covalently to ProteinsEuropean Journal of Biochemistry, 1978
- Purification and Properties of the NAD+: Protein ADP‐ribosyltransferase Responsible for the T4‐Phage‐Induced Modification of the œ Subunit of DNA‐Dependent RNA Polymerase of Escherichia coliEuropean Journal of Biochemistry, 1977
- Poly (ADP-Ribose) and ADP-Ribosylation of ProteinsAnnual Review of Biochemistry, 1977
- Rifampicin-resistant RNA polymerase and NAD transferase activities in coliphage N4 virionsNature, 1976
- Isolation of Preribosomes from HeLa Cells and Their Characterization by Electrophoresis on Uniform and Exponential‐Gradient‐Polyacrylamide GelsEuropean Journal of Biochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- A New Method of Large Scale Preparation of Highly Purified DNA- Dependent RNA-Polymerase fromE. coliHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1970
- Synthesis and assembly of bacterial membrane components: A lipopolysaccharide-phospholipid-protein complex excreted by living bacteriaJournal of Molecular Biology, 1969
- On the formation of a novel adenylic compound by enzymatic extracts of liver nucleiBiochemical and Biophysical Research Communications, 1966
- The hydrolysis of “soluble” ribonucleic acid by snake venom phosphodiesteraseBiochemical and Biophysical Research Communications, 1964