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. 1980 Mar;77(3):1365–1368. doi: 10.1073/pnas.77.3.1365

ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation.

A Ciechanover, H Heller, S Elias, A L Haas, A Hershko
PMCID: PMC348495  PMID: 6769112

Abstract

The heat-stable polypeptide (APF-1) required for ATP-dependent proteolysis in reticulocytes enters into high molecular weight conjugates upon incubation with the fraction of reticulocytes that is retained by DEAE-cellulose. Conjugate formation requires ATP and Mg2+ and its inhibited by N-ethylmaleimide. UTP and GTP are inactive. These properties are identical to those of ATP-dependent protein breakdown in the same system, suggesting that the conjugates are intermediates in this process. The APF-1 conjugates are stable in sodium dodecyl sulfate/polyacrylamide gel electrophoresis and Sephadex G-75 isolation and are resistant to mild acid, alkali, heat denaturation, and reduction; the conjugates are therefore covalent.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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