pH-sensitive interactions between IgG and a mutated IgG-binding protein based upon two B domains of Protein A from Staphylococcus aureus |
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Authors: | Gore, Michael G. Ferris, William F. Popplewell, Andrew G. Scawen, Michael Atkinson, Tony |
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Affiliation: | Department of Biochemistry, SERC Centre for Molecular Recognition, School of Biological Sciences, Bassett Crescent East, University of Southampton Southampton SO9 3TU 1PHLS, Centre for Applied Microbiology and Research Porton, Salisbury, Wiltshire SP4 0JG, UK |
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Abstract: | A fusion protein, consisting of the N-terminal 81 amino acidsfrom an inactive bovine DNase I (Q38,E39E38,Q39) andtwo sequential synthetic IgG-binding domains based upon domainB of Protein A from Staphylococcus aureus has been shown tobind to porcine IgG with a similar affinity and pH profile toProtein A. The same residue in each B domain (Tyr111 and Tyr169)has been mutated by cassette mutagenesis to Ser, Glu, His, Lysor Arg and the effect of the mutation on binding interactionswith porcine IgG investigated. The evidence presented suggeststhat the interactions at the B domain are highly sensitive tothe presence of a charged residue. |
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Keywords: | domain/ IgG/ mutagenesis/ Protein A |
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