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

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Ciechanover, A, Heller, H, Elias, S, Haas, A L, Hershko, A·1980·Proceedings of the National Academy of Sciences

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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Metadata

Authors
Ciechanover, A., Heller, H., Elias, S., Haas, A. L., & Hershko, A.
Venue
Proceedings of the National Academy of Sciences
Published
1980-03
Volume
77
Issue
3
Pages
1365-1368
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2034941135
Cited by
562
References
0
FWCI
6.97
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. https://app.cochat.ai/papers/10.1073/pnas.77.3.1365
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Ciechanover, A., Heller, H., Elias, S., Haas, A. L., & Hershko, A. (1980). ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.77.3.1365

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.