Design of an aprotinin variant with inhibitory activity against chymotrypsin and cathepsin G by recombinant DNA technology.

Article

Design of an aprotinin variant with inhibitory activity against chymotrypsin and cathepsin G by recombinant DNA technology.

Biological chemistry Hoppe-Seyler - 1 May 1990

Brinkmann T, Tschesche H

Abstract excerpt

The [Phe15,17, Glu52]aprotinin gene was constructed from synthetic [Glu52]aprotinin gene by DNA cassette mutagenesis. For substitution of the P1, P'1, P'2 residues of aprotinin (Lys15-Ala16-Arg17) two complementary synthetic oligonucleotides including a new segment coding for the Phe15-Ala16-Phe17 sequence were inserted into the expression vector. The expression was carried out in an E. coli host and [Phe15,17,...

Topics

Amino Acid Sequence
Aprotinin
Base Sequence
Cathepsin G
Cathepsins
Chromatography, High Pressure Liquid
Chymotrypsin
DNA, Recombinant
DNA-Directed DNA Polymerase
Electrophoresis, Polyacrylamide Gel
Escherichia coli

Gene Expression

Genes, Synthetic

Molecular Sequence Data

Mutation

Serine Endopeptidases

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