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Category:1936 births
Category:Date of birth missing
Category:2001 deaths
Category:German physicists
Category:German inventors
Category:Technische Universität Darmstadt alumni
Category:People from Baden-WürttembergExpression and purification of recombinant truncated tardigrade aspartic protease.
Aspartic proteases are ubiquitous enzymes in various animal phyla. Here, we report the design of a recombinant expression system for producing a truncated form of a tardigrade aspartic protease and its purification. The aspartic protease is composed of 423 amino acid residues. To construct the expression vector, we used the sequence encoding a 30-kDa fragment containing the aspartic protease and the purification tag of streptococcal protein G from the C-terminal (Gly-Trp-Ser-Lys-Lys-Lys-Lys-Gly-Gly-Lys-Gly-Gly-Tyr-Lys-Gln-Lys-His-Pro-Lys-Lys-Lys-Gly-Gly-Lys-Lys-Asn-Gly-Gly-Gly-Pro-Ala) and a 35-kDa fragment from the N-terminal (Ser-Asn-Asp-Glu-Thr-Ser-Glu-Glu-Glu-Ser-Ser-Glu-Glu-Asp-Asn-Glu-Glu-Asp-Gly-Gly-Ser-Ser-Ser-His-Gly-Glu-Thr-Ser-Gly-Pro) of the aspartic protease. The expression vector constructed in this study was transformed into Escherichia coli DH5α, and to increase the solubility of the target protein, the recombinant protein was fused with the two tags, streptococcal protein G and maltose-binding protein, via an intervening sequence of a synthetic peptide, Gly-Thr-Ser-Gly-Gly-Gly-Gly-Gly-Ser-Gly. The truncated aspartic protease was purified using affinity chromatography on Affi-Gel-15 coupled with maltose-binding protein. The molecular mass was estimated to be 45.7 kDa, and the N-
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