Mikhaĭlova A G, Shibanova E D, Rumsh L D, Antonov V K
Bioorg Khim. 1994 Aug-Sep;20(8-9):883-93.
Cleavage of different chimeric proteins after specific linker (Asp)4Lys by the highly purified enteropeptidase was investigated, proteins being were accumulated in inclusion bodies or secreted from the cell. Kinetic constants for enzymatic hydrolysis were obtained, indicating that the substrate binding depended mainly on the affinity to the linker peptide (Asp)4Lys. Conditions for the efficient cleavage of recombinant proteins with enteropeptidase are formulated.
研究了高纯度肠肽酶对特定连接子(Asp)4Lys连接的不同嵌合蛋白的切割情况,这些蛋白有的在包涵体中积累,有的从细胞中分泌出来。获得了酶促水解的动力学常数,表明底物结合主要取决于对连接肽(Asp)4Lys的亲和力。制定了用肠肽酶有效切割重组蛋白的条件。