Voprosy meditsinskoi khimii (ISSN 0042-8809)

The inhibition of low molecular substrate hydrolysis by enteropeptidase light chain with chimeric protein IFN-(Asp)4Lys-HIV

   


1. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
PubMed Id: 12698560
Year: 2002 vol: 48  issue:6  pages: 599-602
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 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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Reference: Shibanova E.D., Grishina Yu.B., Rumsh L.D., The inhibition of low molecular substrate hydrolysis by enteropeptidase light chain with chimeric protein IFN-(Asp)4Lys-HIV, Voprosy meditsinskoi khimii, 2002, vol: 48(6), 599-602.
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