Purification and characterization of polynucleotide phosphorylase from Escherichia coli. Probe for the analysis of 3' sequences of RNA.
Open Access
- 1 October 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (19) , 6885-6888
- https://doi.org/10.1016/s0021-9258(17)39932-5
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Globin mRNA Species Containing Poly(A) Segments of Different LengthsEuropean Journal of Biochemistry, 1976
- Readenylation of Polyadenylate‐Free Globin Messenger RNA Restores Its Stability in vivoEuropean Journal of Biochemistry, 1975
- Absence of polyadenylate segment in globin messenger RNA accelerates its degradation in Xenopus oocytes.Proceedings of the National Academy of Sciences, 1975
- Purification of polynucleotide phosphorylase by affinity chromatography and some properties of the purified enzymesNucleic Acids Research, 1974
- In vitro translation of polyadenylic acid-free rabbit globin messenger RNAJournal of Molecular Biology, 1974
- Role of the Polyadenylate Segment in the Translation of Globin Messenger RNA in Xenopus OocytesProceedings of the National Academy of Sciences, 1974
- Quaternary Structure of Polynucleotide Phosphorylase from Escherichia coliEuropean Journal of Biochemistry, 1973
- 18 Polynucleotide PhosphorylasePublished by Elsevier ,1972
- Kinetics of Polymerization and Phosphorolysis Reactions of Escherichia coli Polynucleotide Phosphorylase. Evidence for Multiple Binding of Polynucleotide in PhosphorolysisEuropean Journal of Biochemistry, 1970
- Degradation of transfer ribonucleic acid by polynucleotide phosphorylaseJournal of Molecular Biology, 1967