Highly purified bovine caudate tyrosine hydroxylase can be activated by exposure to enzymatic phosphorylating conditions. This activation is due to both a decrease in the Km for the pterin cofactor and to some increase in Vmax. The Km for the enzyme's substrate, tyrosine, is unchanged by activation. After tyrosine hydroxylase was activated in the presence of [γ-32P]-ATP, no incorporation of 32P into the enzyme was observed by either immunoprecipitation studies or by sucrose gradient studies.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - Oct 6 1975|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology