Stable monomeric form of an originally dimeric serine proteinase inhibitor, ecotin, was constructed via site directed mutagenesis.

Pál, G; Szilágyi, L; Gráf, L

Pál, G; Szilágyi, L; Gráf, L.

Affiliation

Pál G; Department of Biochemistry, Eötvös University, Budapest, Hungary.

FEBS Lett ; 385(3): 165-70, 1996 May 06.

Article in En | MEDLINE | ID: mdl-8647243

Subject(s)

Bacterial Proteins/chemistry; Escherichia coli Proteins; Escherichia coli/chemistry; Mutagenesis, Site-Directed; Periplasmic Proteins; Protein Conformation; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Base Sequence; Chromatography, Affinity; Chromatography, Gel; DNA Primers; Electrophoresis, Agar Gel; Fluorescence; Kinetics; Molecular Sequence Data; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Sequence Deletion; Trypsin/metabolism; Trypsin Inhibitors/chemistry; Tryptophan/chemistry

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Collection: 01-internacional Database: MEDLINE Main subject: Protein Conformation / Bacterial Proteins / Mutagenesis, Site-Directed / Escherichia coli Proteins / Periplasmic Proteins / Escherichia coli Language: En Journal: FEBS Lett Year: 1996 Type: Article Affiliation country: Hungary

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