Development of a convenient spectrophotometric assay for peptide phosphorylation catalyzed by adenosine 3',5'-monophosphate dependent protein kinase
โ Scribed by Bramson, H. Neal; Thomas, Nancy; DeGrado, William F.; Kaiser, E. T.
- Book ID
- 120080061
- Publisher
- American Chemical Society
- Year
- 1980
- Tongue
- English
- Weight
- 337 KB
- Volume
- 102
- Category
- Article
- ISSN
- 0002-7863
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Cyclic AMP-dependent protein kinase is conventionally assayed by measuring the incorporation of radiolabeled phosphate into a histone substrate. Here the assay of the protein kinase is carried out by the positive-ion fast atom bombardment mass spectrometric analysis of the enzyme incubation mixture
A synthetic tetradecapeptide derived from the phosphorylation site of the beta-subunit of phosphorylase kinase (Arg-Thr-Lys-Arg-Ser-Gly-Ser-Val-Tyr-Glu-Pro-Leu-Lys-Ile) is a highly efficient substrate for the cAMP-dependent protein kinase, exhibiting a 36% decrease in the intrinsic tyrosine fluoresc