Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown.

@article{Hershko1983ComponentsOU,
  title={Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown.},
  author={Avram Hershko and Hans Heller and S Elias and Aaron Ciechanover},
  journal={The Journal of biological chemistry},
  year={1983},
  volume={258 13},
  pages={8206-14}
}
By affinity chromatography of a crude reticulocyte extract on ubiquitin-Sepharose, three enzymes required for the conjugation of ubiquitin with proteins have been isolated. One is the ubiquitin-activating enzyme (E1), which is covalently linked to the affinity column in the presence of ATP and can be specifically eluted with AMP and pyrophosphate (Ciechanover, A., Elias, S., Heller, H., and Hershko, A. (1982) J. Biol. Chem. 257, 2537-2542). A second enzyme, designated E2, is bound to the… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 261 extracted citations

Purification and characterization of proteasomes from Saccharomyces cerevisiae.

Current protocols in protein science • 2001
View 2 Excerpts
Highly Influenced

References

Publications referenced by this paper.
Showing 1-2 of 2 references

Annu . Rev . Biochern . ~ ~ ~ 51 , 335364

E. Eytan, A. Ciechanover, A. L. Haas
J . Biol . Chem . • 1982

Protein Turnover and Lysosome Function (Segal

A. Hershko, H. Heller, D. Ganoth, A. Ciechanover
1978

Similar Papers

Loading similar papers…