High performance liquid chromatography resolution of ubiquitin pathway enzymes from wheat germ.

@article{Sullivan1990HighPL,
  title={High performance liquid chromatography resolution of ubiquitin pathway enzymes from wheat germ.},
  author={Michael L Sullivan and Judy Callis and Richard D Vierstra},
  journal={Plant physiology},
  year={1990},
  volume={94 2},
  pages={
          710-6
        }
}
The highly conserved protein ubiquitin is involved in several cellular processes in eukaryotes as a result of its covalent ligation to a variety of target proteins. Here, we describe the purification of several enzymatic activities involved in ubiquitin-protein conjugate formation and disassembly from wheat germ (Triticum vulgare) by a combination of ubiquitin affinity chromatography and anion-exchange high performance liquid chromatography. Using this procedure, ubiquitin activating enzyme (E1… CONTINUE READING
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