HEAT-STABLE POLYPEPTIDE COMPONENT OF AN ATP-DEPENDENT PROTEOLYTIC SYSTEM FROM RETICULOCYTES
HEAT-STABLE POLYPEPTIDE COMPONENT OF AN ATP-DEPENDENT PROTEOLYTIC SYSTEM FROM RETICULOCYTES
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DOI：
10.1016/0006-291x(78)91249-4
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发表时间：
1978-01-01
影响因子：
3.1
通讯作者：
HERSHKO, A
中科院分区：
文献类型：
--
作者：
CIECHANOVER, A;HOD, Y;HERSHKO, A
ATP对兔网织红细胞裂解液中变性珠蛋白的降解有明显的促进作用。该系统现在被分解成2个组分，指定为级分I和II，以它们从DEAE-纤维素洗脱的顺序。组分II具有中性蛋白酶活性，但仅受ATP轻微刺激，而组分I没有蛋白水解活性，但当与组分II组合时恢复ATP依赖性蛋白水解。级分I的活性成分是显著热稳定的，但它是不可透析的，用硫酸铵可沉淀，并且它通过用蛋白水解酶处理而被破坏。在Sephadex-G-75凝胶过滤中，它表现为MW约为9000的单一组分。
The degradation of denatured globin in rabbit reticulocyte lysates is markedly stimulated by ATP. This system was now resolved into 2 components, designated fractions I and II, in the order of their elution from DEAE-cellulose. Fraction II has a neutral protease activity but is stimulated only slightly by ATP, whereas fraction I has no proteolytic activity but restores ATP-dependent proteolysis when combined with fraction II. The active principle of fraction I is markedly heat-stable, but it is non-dialysable, precipitable with ammonium sulfate and it is destroyed by treatment with proteolytic enzymes. In gel filtration on Sephadex-G-75, it behaves as a single component with a MW of approximately 9000.