Abstract
The two major forms of rat liver phenylalanine hydroxylase have been isolated and partially purified. The tetrahydrobiopterin-dependent activity of these forms can be differentially stimulated by exposure to enzymatic phosphorylating conditions. This in vitro treatment is associated with incorporation of 32p into the enzymes and generates a further, chromatographically distinct, species. These results suggest that the multiple forms of rat liver phenylalanine hydroxylase are due to different degrees of phosphorylation.
| Original language | English |
|---|---|
| Pages (from-to) | 1011-1017 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 78 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 10 Oct 1977 |
| Externally published | Yes |
Fingerprint
Dive into the research topics of 'Modification of the multiple forms of rat hepatic phenylalanine hydroxylase by in vitro phosphorylation'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver