title: [Enteropeptidase and its use for cleavage of chimeric proteins].
abstract: 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.
authors: A G
authors: AG
authors: Mikhaĭlova
authors: E D
authors: ED
authors: Shibanova
authors: L D
authors: LD
authors: Rumsh
authors: V K
authors: VK
authors: Antonov
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004743:Enkephalin, Leucine / Q000378:metabolism; D004765:Enteropeptidase / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D002479:Inclusion Bodies / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity; D001616:beta-Galactosidase / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D004743:Enkephalin, Leucine; D001616:beta-Galactosidase; D004765:Enteropeptidase
vernacular_title: Enteropeptidaza i ee primenenie dlia rasshepleniia khimernykh belkov.