ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation.
A Ciechanover, H Heller, S Elias… - Proceedings of the …, 1980 - National Acad Sciences
A Ciechanover, H Heller, S Elias, AL Haas, A Hershko
Proceedings of the National Academy of Sciences, 1980•National Acad SciencesThe 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 …
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 …
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.
National Acad Sciences