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Effect of high pressure on activity of rabbit reticulocyte cell-free protein-synthesizing system

机译：高压对兔网织红细胞无蛋白合成系统活性的影响

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摘要

Studies so far indicate that many processes in the interactions between biomacromole-cules are accompanied by a change in occupied volume. For instance, the association of protein subunits into oligomer and the formation of protein-nucleic acid complex give an increase in volume. The increase in volume in these processes mainly results from: (i) the formation of the dead space between the subunits of the oligomeric protein or the complexes in the processes mentioned above; (ii) the formation of saltbonds and (iii) the interactions between hydrophobic groups. It is known from the Lechatelier principle that if high pressure is applied to an equilibrium system mentioned above, the original equilibrium will be changed, resulting in promoting the dissociation, an opposite way of association, Many experiments have already proved that when the applied hydrostatic pressure is lower than 3 x 10~8 Pa, the single chain protein is still in native conformational state without denaturation. So the high hydrostatic pressure technology provides a new approach to study biomacromolecules without damage. A lot of works about it have been reported abroad. The protein biosynthesis is mainly carried out in ribosomes. It is known that the ribosome consists of a large subunit and a small subunit. And these subunits consist of protein subunits and rRNAs. Infante and Baierlein studied the ribosome dissociation using the pressure generated from ultracentrifuge and obtained some thermodynamic parameters about the dissociation. But up to now there has been no report about the effect of high pressure on the biological activity of ribosomes. In this note the rabbit reticulocyte cell-free protein-synthesizing system is used as an object to study the effect of high pressure on protein-synthesizing activity.
机译：迄今为止的研究表明，生物大分子与分子之间相互作用的许多过程都伴随着占有体积的变化。例如，蛋白质亚基缔合为低聚物和蛋白质-核酸复合物的形成增加了体积。这些过程中体积的增加主要是由于：（i）在上述过程中寡聚蛋白的亚基或复合物之间形成了死区; （ii）盐键的形成和（iii）疏水基团之间的相互作用。从Lechatelier原理可知，如果对上述平衡系统施加高压，则原始平衡会发生变化，从而促进离解，这是相反的缔合方式。许多实验已经证明，当施加静水压力时低于3 x 10〜8 Pa，单链蛋白仍处于天然构象状态而没有变性。因此，高静水压技术为研究生物大分子无损伤提供了一种新方法。国外已报道了许多有关它的作品。蛋白质的生物合成主要在核糖体中进行。已知核糖体由大的亚基和小的亚基组成。这些亚基由蛋白质亚基和rRNA组成。 Infante和Baierlein使用超速离心机产生的压力研究了核糖体的解离，并获得了有关解离的一些热力学参数。但是到目前为止，还没有关于高压对核糖体生物活性的影响的报道。在本文中，兔无网织红细胞无蛋白合成系统被用作研究高压对蛋白合成活性的影响的对象。

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