The dephosphorylation of 32P-tetradecapeptide derived from phosphorylase a is described. The rate of enzymatic dephosphorylation by phosphatase is inhibited in the presence of phosphorylase b. Phosphorylase b′, a modified form of phosphorylase a in which the phosphorylated site has been removed by tryptic attack, can increase the liberation of 32P from the tetradecapeptide. The deprohosphorylation also shows ligand sensitivity in the presence of phosphorylase b′. AMP is inhibitory, glucose and glucose 6-P can abolish the AMP inhibition. The complex of phosphorylase b′ and tetradecapeptide could form also a tetramer supported by dephosphorylation studies at 15°.
|Number of pages||7|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - May 14 1980|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology