Limited proteolysis of N-(5′-phosphoribosyl)anthranilate isomerase: Indoleglycerol phosphate synthase from Escherichia coli yields two different enzymically active, functional domains
- 1 November 1980
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 143 (4) , 395-409
- https://doi.org/10.1016/0022-2836(80)90219-3
Abstract
No abstract availableFunding Information
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (3.412-0.78)
This publication has 45 references indexed in Scilit:
- A functional hybrid ribosome binding site in tryptophan operon messenger RNA of Escherichia coliJournal of Molecular Biology, 1980
- N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 1. A substrate analog binds to two different binding sites on the bifunctional enzyme from Escherichia coliBiochemistry, 1979
- N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 2. Fast-reaction studies show that a fluorescent substrate analog binds independently to two different sitesBiochemistry, 1979
- Gel filtration of proteins on sephacryl® S‐200 superfine in 6 M guanidine‐HClFEBS Letters, 1978
- Influence of single amino acid substitutions on electrophoretic mobility of sodium dodecyl sulfate-protein complexesBiochemical and Biophysical Research Communications, 1978
- Abnormal Behaviour of Proline in the Isothiocyanate DegradationHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- Analysis of bacteriophage T7 early RNAs and proteins on slab gelsJournal of Molecular Biology, 1973
- The large scale preparation of chromatographic grade hydroxylapatite and its application in protein separation proceduresJournal of Chemical Technology & Biotechnology, 1973
- Rapid and effective removal of sodium dodecyl sulfate from proteinsBiochemical and Biophysical Research Communications, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970