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 effeciently. The resistant to the hydrolysis chimeric protein IFN-(Asp)4Lys-HIV earlier was shown to be the competitive inhibitor (Ki=3,4х10-6М) 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=2,7х10-5М). Comparison the Ki values for the substrate hydrolysis by full lengh enzyme and it's light chain promoted to suggest that the enteropeptidase heavy chain may participate in chimeric protein binding
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Shibanova E.D., Grishina Yu.B., Rumsh L.D. (2002) The inhibition of low molecular substrate hydrolysis by enteropeptidase light chain with chimeric protein IFN-(Asp)4Lys-HIV. Voprosy Meditsinskoi Khimii, 48(6), 599-602.
Shibanova E.D. et al. The inhibition of low molecular substrate hydrolysis by enteropeptidase light chain with chimeric protein IFN-(Asp)4Lys-HIV // Voprosy Meditsinskoi Khimii. - 2002. - V. 48. -N 6. - P. 599-602.
Shibanova E.D. et al., "The inhibition of low molecular substrate hydrolysis by enteropeptidase light chain with chimeric protein IFN-(Asp)4Lys-HIV." Voprosy Meditsinskoi Khimii 48.6 (2002): 599-602.
Shibanova, E. D., Grishina, Yu. B., Rumsh, L. D. (2002). The inhibition of low molecular substrate hydrolysis by enteropeptidase light chain with chimeric protein IFN-(Asp)4Lys-HIV. Voprosy Meditsinskoi Khimii, 48(6), 599-602.
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