Patent
Protein capable of binding specifically to immunoglobulin, and immunoglobulin-binding affinity ligand
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TLDR
In this article, a protein having an affinity for an immunoglobulin, including an amino acid sequence obtained by introducing, into the amino acid sequences derived from any of E, D, A, B and C domains of Protein A, at least one amino acid substitution at any one or more of amino acid residues corresponding to positions 31 to 37 of the A and B domains, which are conserved in all the domains.Abstract:
An object of the present invention is to create a novel engineered Protein A ligand having better antibody dissociation properties in the acidic condition compared with known engineered Protein A ligands. The present invention provides a protein having an affinity for an immunoglobulin, including an amino acid sequence obtained by introducing, into an amino acid sequence derived from any of E, D, A, B and C domains of Protein A, at least one amino acid substitution at any one or more of amino acid residues corresponding to positions 31 to 37 of the A, B and C domains (positions 29 to 35 of the E domain, positions 34 to 40 of the D domain), which are conserved in all the domains, the protein having a lower affinity for an Fab region of an immunoglobulin than a protein having the amino acid sequence before introduction of the substitution.read more
Citations
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Mechanism of antibodies purification by protein A.
TL;DR: This review has focused on the study of both native and engineered Protein A to understand its mechanism in the purification of antibodies to find interesting and stimulating answers to all questions.
Patent
Mutated immunoglobulin-binding polypeptides
TL;DR: In this article, a polypeptide with improved alkaline stability was revealed, which polyptide comprises a mutant of a B or C domain of Staphylococcus Protein A (SpA), as specified by SEQ ID NO 1 or SEQID NO 2, or of Protein Z, wherein at least the glutamine residue at position 9 has been mutated to an amino acid other than asparagine.
Patent
Protein for affinity-separation matrix
TL;DR: In this article, an engineered protein having a sequence obtained by replacing all the lysine residues in Protein A, which is the most typical protein ligand, with other amino acids, and adding Lysine at a terminal is presented.
Patent
Affinity chromatography matrix
TL;DR: In this article, a method of separating one or more immunoglobulin containing proteins from a liquid is proposed. But the method is not suitable for the handling of large amounts of liquid.
Patent
Protein ligand for affinity isolation matrix
Shinichi Yoshida,Dai Murata,Fuminori Konoike,Keita Iguchi,Tomoyuki Nakaishi,Masahiro Hayashi +5 more
TL;DR: In this article, the problem of developing modified protein ligands that maximize binding capacity and binding efficiency to a target molecule when a protein ligand is immobilized in an affinity isolation matrix is addressed.
References
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Journal ArticleDOI
A synthetic IgG-binding domain based on staphylococcal protein A
Björn Nilsson,Tomas Moks,Birger Jansson,Lars Abrahmsén,Anette Elmblad,Erik Holmgren,Christina Henrichson,T. Alwyn Jones,Mathias Uhlén +8 more
TL;DR: In this paper, a synthetic IgG-binding domain based on staphylococcal protein A was designed with the aid of sequence comparisons and computer graphic analysis to overcome the difficulties of introducing site-specific changes into the repetitive gene.
Journal ArticleDOI
Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: Structural basis for recognition of B-cell receptors and superantigen activity
Marc Graille,Enrico A. Stura,A.L. Corper,Brian J. Sutton,Michael J. Taussig,Jean-Baptiste Charbonnier,Gregg J. Silverman +6 more
TL;DR: Staphylococcus aureus produces a virulence factor, protein A (SpA), that contains five homologous Ig-binding domains that rely on a sequence-restricted conformational binding with residue side chains, suggesting that this common bacterial pathogen has adopted distinct molecular recognition strategies for affecting large sets of B and T lymphocytes.
Journal ArticleDOI
Protein A chromatography for antibody purification
TL;DR: A minimized SPA derivative has been constructed and a domain originating from SPA has been improved to withstand the harsh environment employed in industrial purifications.
Journal ArticleDOI
Future of antibody purification.
TL;DR: A wide survey of technologies that are competing to be part of a platform, and an assessment of those that have the most promise are provided.
Journal ArticleDOI
Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat.
TL;DR: Structural and calorimetric data indicate that, despite its modular structure, the Notch ankyrin domain unfolds as a cooperative unit consisting of the six C-terminal repeats, and that this cooperativity is maintained in the presence of severely destabilizing substitutions in the N-Terminal and central repeats.