A new procedure has been developed for the purification of tyrosine hydroxylase from bovine caudate nucleus. This procedure yields a soluble and stable enzyme which has been purified 50-fold from an acetone powder extract. The enzyme is stimulated greater than 3-fold by phosphatidyl-L-serine and other polyanions which lower the Km of the enzyme for the pterin cofactor. Substrate inhibition and an ability to readily hydroxylate phenylalanine in the presence of tetrahydrobiopterin have also been observed with this preparation.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Aug 19 1974|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology