ATP-DEPENDENT CONJUGATION OF RETICULOCYTE PROTEINS WITH THE POLYPEPTIDE REQUIRED FOR PROTEIN-DEGRADATION
ATP-DEPENDENT CONJUGATION OF RETICULOCYTE PROTEINS WITH THE POLYPEPTIDE REQUIRED FOR PROTEIN-DEGRADATION
复制标题
DOI：
10.1073/pnas.77.3.1365
复制
发表时间：
1980-01-01
期刊：
影响因子：
--
通讯作者：
HERSHKO, A
中科院分区：
文献类型：
--
作者：
CIECHANOVER, A;HELLER, H;HERSHKO, A
[兔]网织红细胞中ATP依赖性蛋白水解所需的热稳定多肽（APF-1）在与被DEAE-纤维素保留的网织红细胞部分孵育后进入高MW缀合物。结合物的形成需要ATP和Mg 2+，并被N-乙基马来酰亚胺抑制。UTP和GTP不活动。这些性质与相同系统中ATP依赖性蛋白质分解的性质相同，表明缀合物是该过程中的中间体。APF-1结合物在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳和Sephadex G-75分离中稳定，并且耐弱酸、碱、热变性和还原;因此结合物是共价的。
The heat-stable polypeptide (APF-1) required for ATP-dependent proteolysis in [rabbit] reticulocytes enters into high MW conjugates upon incubation with the fraction of reticulocytes that is retained by DEAE-cellulose. Conjugate formation requires ATP and Mg2+ and is 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.