In vitro selection for catalytic turnover from a library of β-lactamase mutants and penicillin-binding proteins
- 18 February 1997
- journal article
- Published by Elsevier in Bioorganic & Medicinal Chemistry Letters
- Vol. 7 (4) , 479-484
- https://doi.org/10.1016/s0960-894x(97)00040-1
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Selection of the most active enzymes from a mixture of phage-displayed β-lactamase mutantsBioorganic & Medicinal Chemistry Letters, 1996
- Random mutagenesis of staphylococcal nuclease and phage display selectionBioorganic & Medicinal Chemistry, 1995
- Glutathione Transferases with Novel Active Sites Isolated by Phage Display from a Library of Random MutantsJournal of Molecular Biology, 1995
- Contribution of mutant analysis to the understanding of enzyme catalysis: The case of class A β-lactamasesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- Site-directed mutagenesis of β-lactamase I: role of Glu-166Biochemical Journal, 1994
- Selection of β-Lactamase on Filamentous Bacteriophage by Catalytic ActivityJournal of Molecular Biology, 1994
- Phage-enzymes: expression and affinity chromatography of functional alkaline phosphatase on the surface of bacteriophageProtein Engineering, Design and Selection, 1991
- Phage antibodies: filamentous phage displaying antibody variable domainsNature, 1990
- Hormone phage: An enrichment method for variant proteins with altered binding propertiesProteins-Structure Function and Bioinformatics, 1990
- Filamentous Fusion Phage: Novel Expression Vectors That Display Cloned Antigens on the Virion SurfaceScience, 1985