[Enteropeptidase and its use for cleavage of chimeric proteins].
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.
Mikhaĭlova
A G
AG
Shibanova
E D
ED
Rumsh
L D
LD
Antonov
V K
VK
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
D011994:Recombinant Proteins; D004743:Enkephalin, Leucine; D001616:beta-Galactosidase; D004765:Enteropeptidase
Enteropeptidaza i ee primenenie dlia rasshepleniia khimernykh belkov.