Expression, purification, characterization, and deletion mutations of phosphorylase kinase γ subunit: identification of an inhibitory domain in the γ subunit

@article{Huang2005ExpressionPC,
  title={Expression, purification, characterization, and deletion mutations of phosphorylase kinase $\gamma$ subunit: identification of an inhibitory domain in the $\gamma$ subunit},
  author={Chi-Ying F. Huang and Chiun-Jye Yuan and Nataliya B. Livanova and Donald J. Graves},
  journal={Molecular and Cellular Biochemistry},
  year={2005},
  volume={127-128},
  pages={7-18}
}
A catalytic fragment,γ1-298, derived from limited chymotryptic digestion of phosphorylaseb kinase (Harris, W.R.et al., J. Biol. Chem., 265: 11740–11745, 1990), is reported to have about six-fold greater specific activity than does the γ subunit-calmodulin complex. To test whether there is an inhibitory domain located outside the catalytic core of the γ subunit, full-length wild-type and seven truncated forms of γ were expressed inE. coli. Recombinant proteins accumulate in the inclusion bodies… 
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TLDR
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