[Hydrolysis of chimeric proteins by enteropeptidase at the specific linker (Asp)4Lys depending on refolding conditions].
Refolding from inclusion bodies of chimeric proteins containing the enteropeptidase-specific linker (Asp)4Lys was carried out. It was shown that, depending on the refolding conditions, chimeric proteins function as substrates or inhibitors of the enteropeptidase. The efficiency of the enteropeptidase hydrolysis of chimeric proteins containing the (Asp)4Lys linker may depend not only on the amino acid sequence of the protein binding site for the enzyme but also on the site conformation.
Shibanova
E D
ED
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia. shib@enzyme.siobc.ras.ru
Mikhaĭlova
A G
AG
Aleksandrov
S L
SL
Rumsh
L D
LD
D001224:Aspartic Acid / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004765:Enteropeptidase / Q000737:chemistry*; D006868:Hydrolysis; D002479:Inclusion Bodies / Q000737:chemistry; D007700:Kinetics; D008239:Lysine / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
D011993:Recombinant Fusion Proteins; D001224:Aspartic Acid; D004765:Enteropeptidase; D008239:Lysine