The activation of rat liver phenylalanine hydroxylase by limited proteolysis, lysolecithin, and tocopherol phosphate. Changes in conformation and catalytic properties.
Open Access
- 1 December 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (23) , 14560-14566
- https://doi.org/10.1016/s0021-9258(17)42637-8
Abstract
No abstract availableThis publication has 34 references indexed in Scilit:
- Spectroscopic investigation of ligand interaction with hepatic phenylalanine hydroxylase: evidence for a conformational change associated with activationBiochemistry, 1984
- Ligand effects on the limited proteolysis of phenylalanine hydroxylase: Evidence for multiple conformational statesBiochemical and Biophysical Research Communications, 1983
- Mechanism of action of phenylalanine hydroxylaseBiochemistry, 1981
- On the phosphate content of rat liver phenylalanine hydroxylase purified by hydrophobic chromatographyBiochemical and Biophysical Research Communications, 1981
- Determination of the helix and β form of proteins in aqueous solution by circular dichroismBiochemistry, 1974
- Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersionBiochemistry, 1972
- Stimulation of rat liver phenylalanine hydroxylase activity by derivatives of vitamin EBiochemical and Biophysical Research Communications, 1972
- A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroismBiochemical and Biophysical Research Communications, 1971
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969
- Rat Liver Phenylalanine HydroxylaseEuropean Journal of Biochemistry, 1969