Reversible dissociation of tryptophanase into protein subunits.
- 1 October 1966
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 56 (4) , 1223-1225
- https://doi.org/10.1073/pnas.56.4.1223
Abstract
Tryptophanase is dissociable into enzymatically inactive protein subunits which are 1/2 the size of the active enzyme as deduced from their behavior in sucrose density gradient sedimentation experiments. Dissociation of tryptophanase is facilitated by Trls; aggregation to the active enzyme is facilitated by K3(PC4).Keywords
This publication has 4 references indexed in Scilit:
- Protein synthesis and ribosome-bound tryptophanaseJournal of Molecular Biology, 1965
- Properties of Crystalline TryptophanaseJournal of Biological Chemistry, 1965
- Properties of tryptophanase from Escherichia coliBiochimica et Biophysica Acta, 1962
- A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein MixturesJournal of Biological Chemistry, 1961