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Mutated immunoglobulin-binding protein
KTH, School of Biotechnology (BIO), Proteomics (closed 20130101).ORCID iD: 0000-0003-0605-8417
2002 (English)Patent (Other (popular science, discussion, etc.))
Abstract [en]

The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.

Place, publisher, year, edition, pages
2002.
National Category
Industrial Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-87882OAI: oai:DiVA.org:kth-87882DiVA: diva2:501985
Patent
EP 1485407-B1 (2009-05-13)
Note

JP 4391830-B2 (2009-12-24); AU 2003217119-B2 (2010-02-18); US 7834158-B2 (2010-11-16); CN 1642976-B (2012-02-22); US 8198404-B2 (2012-06-12); EP 1485407-B2 (2012-09-26); US 8354510-B2 (2013-01-15); CN 102532284 B (2014-04-16)

Available from: 2012-02-14 Created: 2012-02-14 Last updated: 2015-05-12Bibliographically approved

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Hober, Sophia

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