Topchieva I N, Snitko Ia E, Efremova N V, Sorokina E M
Biokhimiia. 1995 Jan;60(1):131-6.
The ability of alpha-chymotrypsin to form complexes with amphiphilic block copolymer of ethylene oxide and propylene oxide upon heating up to 44-60 degrees C has been demonstrated for the first time. Depending on temperature and the initial component ratio, some complexes were obtained which varied in both composition and enzymatic activity. With a rise in the complexation temperature, the polymer content in the complex increased, while the enzymatic activity of the complex decreases. The complexes are very stable in water, but dissociate in 8 M urea and are characterized by enhanced thermal stability as compared with the original enzyme. It is assumed that both hydrophobic interactions and hydrogen bonds between the components are involved in the complex formation.
首次证明了α-胰凝乳蛋白酶在加热至44-60摄氏度时与环氧乙烷和环氧丙烷的两亲性嵌段共聚物形成复合物的能力。根据温度和初始组分比例，得到了一些在组成和酶活性上都有所不同的复合物。随着络合温度的升高，复合物中的聚合物含量增加，而复合物的酶活性降低。这些复合物在水中非常稳定，但在8M尿素中会解离，并且与原始酶相比具有更高的热稳定性。据推测，复合物的形成涉及组分之间的疏水相互作用和氢键。
