Kuehl L, Robison W
Biochim Biophys Acta. 1979 Jul 26;563(2):454-65. doi: 10.1016/0005-2787(79)90064-9.
The peptidyl transferase reaction, as measured by the formation of peptidyl-puromycin, was compared for free ribosomes and ribosomes bound to two types of membrane, the endoplasmic reticulum and the outer nuclear membrane. In most respects the reaction catalyzed by the three types of ribosome was similar, demonstrating that interaction of the 60 S ribosomal subunit with the membrane has little effect on the functioning of peptidyl transferase, a 60 S protein. However, both the rate and extent of synthesis of peptidyl puromycin were lower for ribosomes bound to the nuclear membrane than for free or microsome-bound ribosomes. This difference appears to be a direct consequence of the ribosome-membrane interaction, since ribosomes stripped from the nuclear membrane could not be distinguished from the other classes of ribosome.
通过肽基嘌呤霉素的形成来测定肽基转移酶反应，对游离核糖体以及与两种膜（内质网和外核膜）结合的核糖体进行了比较。在大多数方面，这三种类型核糖体催化的反应是相似的，表明60S核糖体亚基与膜的相互作用对肽基转移酶（一种60S蛋白质）的功能影响很小。然而，与核膜结合的核糖体合成肽基嘌呤霉素的速率和程度均低于游离核糖体或与微粒体结合的核糖体。这种差异似乎是核糖体 - 膜相互作用的直接结果，因为从核膜上剥离的核糖体与其他类型的核糖体并无区别。
