[Inhibition by IFN-(Asp)4-Lys-HIV chimeric protein of hydrolysis of the low molecular substrate by the enteropeptidase light chain].

Abstract

The full length enteropeptidase or it's light chain have often used for the limited proteolysis of recombinant chimeric proteins incorporating the linker-(Asp)4Lys- to obtain the target protein. Any chimeric proteins were not cleaved by the full length enteropeptidase efficiently. The resistant to the hydrolysis chimeric protein IFN-(Asp)4Lys-HIV earlier was shown to be the competitive inhibitor (Ki = 3,4 x 10(-6) M) in relation to the low molecular substrate. In present study we were determined this chimeric protein competitive inhibited the same substrate hydrolysis by enteropeptidase light chain (Ki = 2,7 x 10(-5) M). Comparison the Ki values for the substrate hydrolysis by full length enzyme and its light chain suggests that the enteropeptidase heavy chain may participate in chimeric protein binding.