Granted Patent
B2
US 12,486,307 · App. 17/388,090 · Granted Dec 2, 2025
Caustic stable chromatography ligands
Inventors:
Nanying Bian (Lexington, MA); Neil Soice (Simi Valley, CA); Shari Spector (Lexington, MA); Kara Levine (Worcester, MA)
Assignee:
EMD Millipore Corporation
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Abstract
The present invention relates to chromatography ligands having improved caustic stability, e.g., ligands based on immunoglobulin-binding proteins such as, Staphylococcal protein A, as well as methods of making and using such ligands.
Claims (11)
1 . An alkaline-stable chromatography ligand comprising two or more Z domains of Staphylococcus protein A (SpA) attached to a chromatography resin at more than one site on the resin, wherein each Z domain comprises the amino acid sequence set forth in SEQ ID NO: 12 having a mutation to replace the amino acid at position 29 with an amino acid other than alanine or tryptophan to reduce Fab binding, wherein the ligand retains at least 95% of its binding capacity after 5 hours incubation in 0.5 M NaOH.
2 . The alkaline-stable chromatography ligand of claim 1 , wherein the ligand comprises three or more Z domains.
3 . The alkaline-stable chromatography ligand of claim 1 , wherein the ligand comprises four or more Z domains.
4 . The alkaline-stable chromatography ligand of claim 1 , wherein the ligand comprises five or more Z domains.
5 . The alkaline-stable chromatography ligand of claim 1 , wherein the ligand comprises six or more Z domains.
6 . The alkaline-stable chromatography ligand of claim 1 , wherein the ligand comprises seven or more Z domains.
7 . A chromatography matrix comprising a ligand according to claim 1 .
8 . The ligand according to claim 1 , wherein the ligand is capable of binding at least 1.5 times, or 2 times, or 3 times, or more of IgG as compared to wild type (wt) SpA, following exposure to 0.5M NaOH for at least 5 hours.
9 . A caustic stable affinity chromatography matrix comprising a ligand comprising three or more, or four or more, or five or more, or six or more, or seven or more Z domains of Staphylococcus protein A (SpA) attached to a solid support via multipoint attachment, wherein each Z domain comprises the amino acid sequence set forth in SEQ ID NO: 12 having a mutation to replace the amino acid at position 29 with an amino acid other than alanine or tryptophan to reduce Fab binding, wherein the ligand retains at least 95% of its binding capacity after 5 hours incubation in 0.5 M NaOH.
10 . The caustic stable chromatography matrix of claim 9 , wherein the solid support is selected from the group consisting of controlled pore glass, polyvinyl alcohol, zirconium oxide, agarose, polymethacrylate, polyacrylate, polyacrylamide and polystyrene.
11 . The caustic stable affinity chromatography ligand of claim 1 comprising three Z domains (Z3) or four Z domains (Z4), or five Z domains (Z5), or six Z domains (Z6), or seven Z domains (Z7) of Staphylococcus protein A (SpA) attached to a solid support wherein the extent of caustic stability of ligand is in the order of Z3<Z4<Z5<Z6<Z7, following exposure of ligand to 0.5M NaOH for at least 5 hours.
Continuity (4)
Provisional Application
61203664
· Dec 24, 2008
References Cited (207)
US 4617266A
· Fahnestock
· 1986
[cited by applicant]
US 4879378A
· Foster et al.
· 1989
[cited by applicant]
US 5084559A
· Profy
· 1992
[cited by applicant]
US 5143844A
· Abrahmsen et al.
· 1992
[cited by applicant]
US 5151350A
· Colbert et al.
· 1992
[cited by applicant]
US 5198531A
· Webber et al.
· 1993
[cited by applicant]
US 5240680A
· Zuckermann et al.
· 1993
[cited by applicant]
US 5260373A
· Profy et al.
· 1993
[cited by applicant]
US 5580757A
· Desnick et al.
· 1996
[cited by applicant]
US 6013763A
· Braisted et al.
· 2000
[cited by applicant]
US 6060596A
· Lerner et al.
· 2000
[cited by applicant]
US 6197927B1
· Braisted et al.
· 2001
[cited by applicant]
US 6399750B1
· Johansson
· 2002
[cited by applicant]
US 6602977B1
· Ljungqvist et al.
· 2003
[cited by applicant]
US 6831161B1
· Uhlen et al.
· 2004
[cited by applicant]
US 7026446B1
· Atwell et al.
· 2006
[cited by applicant]
US 7083948B1
· Sassenfeld et al.
· 2006
[cited by applicant]
US 7163686B1
· Silverman
· 2007
[cited by applicant]
US 7192738B2
· Lowman et al.
· 2007
[cited by applicant]
US 7311918B2
· Choi et al.
· 2007
[cited by applicant]
US 7691608B2
· Peyser
· 2010
[cited by applicant]
US 7709209B2
· Hober et al.
· 2010
[cited by applicant]
US 7833723B2
· Bian et al.
· 2010
[cited by applicant]
US 7834158B2
· Hober
· 2010
[cited by applicant]
US 7846682B2
· Bian et al.
· 2010
[cited by applicant]
US 7847071B2
· Bonnerjea et al.
· 2010
[cited by applicant]
US 8329860B2
· Hall et al.
· 2012
[cited by applicant]
US 8592555B2
· Spector
· 2013
[cited by applicant]
US 8754196B2
· Spector et al.
· 2014
[cited by applicant]
US 9920112B2
· Spector
· 2018
[cited by examiner]
US 20030059910A1
· Moloney et al.
· 2003
[cited by applicant]
US 20050100970A1
· Uhlen et al.
· 2005
[cited by applicant]
US 20050143566A1
· Hober
· 2005
[cited by applicant]
US 20050171339A1
· Sugo et al.
· 2005
[cited by applicant]
US 20060030696A1
· Bonnerjea et al.
· 2006
[cited by applicant]
US 20060194950A1
· Hober et al.
· 2006
[cited by applicant]
US 20060194955A1
· Hober et al.
· 2006
[cited by applicant]
US 20060205016A1
· Silverman
· 2006
[cited by applicant]
US 20070148131A1
· Mrsny
· 2007
[cited by applicant]
US 20070207500A1
· Bian et al.
· 2007
[cited by applicant]
US 20080096819A1
· Grabstein et al.
· 2008
[cited by applicant]
US 20080108053A1
· Patchomnik
· 2008
[cited by applicant]
US 20080210615A1
· Joehnck et al.
· 2008
[cited by applicant]
US 20080255027A1
· Moya et al.
· 2008
[cited by applicant]
US 20080312425A1
· Bonnerjea et al.
· 2008
[cited by applicant]
US 20090093017A1
· Peyser
· 2009
[cited by applicant]
US 20090299035A1
· Twakura et al.
· 2009
[cited by applicant]
US 20090317381A1
· Plaut et al.
· 2009
[cited by applicant]
US 20100022760A1
· Hober et al.
· 2010
[cited by applicant]
US 20100048876A1
· Hall et al.
· 2010
[cited by applicant]
US 20100130721A1
· Iwakura et al.
· 2010
[cited by applicant]
US 20100168395A1
· Sato
· 2010
[cited by applicant]
US 20120149875A1
· Johansson et al.
· 2012
[cited by applicant]
CN 1642976A
· 2005
[cited by applicant]
CN 1649894A
· 2005
[cited by applicant]
CN 101522278A
· 2009
[cited by applicant]
CN 101704879A
· 2010
[cited by applicant]
CN 101775069A
· 2010
[cited by applicant]
CN 103601794A
· 2014
[cited by applicant]
CN 108912216A
· 2018
[cited by applicant]
EP 0230869A2
· 1987
[cited by applicant]
EP 0550771A1
· 1993
[cited by applicant]
EP 1564286A1
· 2005
[cited by applicant]
EP 1123389B1
· 2005
[cited by applicant]
EP 1601697B1
· 2007
[cited by applicant]
EP 1972689A2
· 2008
[cited by applicant]
EP 1992692A1
· 2008
[cited by applicant]
EP 2014359A1
· 2009
[cited by applicant]
EP 2066419A1
· 2009
[cited by applicant]
EP 2157099A1
· 2010
[cited by applicant]
EP 2202310A2
· 2010
[cited by applicant]
JP 2005220028A
· 2005
[cited by applicant]
JP 2005538693A
· 2005
[cited by applicant]
JP 2006304633A
· 2006
[cited by applicant]
JP 2007525412A
· 2007
[cited by applicant]
JP 2007252368A
· 2007
[cited by applicant]
JP 2007537700A
· 2007
[cited by applicant]
JP 2008255046A
· 2008
[cited by applicant]
JP 200971766A
· 2009
[cited by applicant]
JP 5480558B2
· 2014
[cited by applicant]
RU 2415865C2
· 2011
[cited by applicant]
WO 8400773A1
· 1984
[cited by applicant]
WO 9002182A1
· 1990
[cited by applicant]
WO 9009237A1
· 1990
[cited by applicant]
WO 95019374A1
· 1995
[cited by applicant]
WO 9717361A1
· 1997
[cited by applicant]
WO 9736614A1
· 1997
[cited by applicant]
WO 0023580A1
· 2000
[cited by applicant]
WO 0063243A1
· 2000
[cited by applicant]
WO 0069457A1
· 2000
[cited by applicant]
WO 03080655A1
· 2003
[cited by applicant]
WO 2004076485A1
· 2004
[cited by applicant]
WO 2005003156A1
· 2005
[cited by applicant]
WO 2006004067A1
· 2006
[cited by applicant]
WO 2006070416A1
· 2006
[cited by applicant]
WO 2006092338A2
· 2006
[cited by applicant]
WO 2007019376A2
· 2007
[cited by applicant]
WO 2007138328A2
· 2007
[cited by applicant]
WO 2008039141A1
· 2008
[cited by applicant]
WO 2008091740A2
· 2008
[cited by applicant]
WO 2008127457A2
· 2008
[cited by applicant]
WO 2009138484A2
· 2009
[cited by applicant]
WO 2009146755A1
· 2009
[cited by applicant]
WO 2010080065A1
· 2010
[cited by applicant]
WO 2010110288A1
· 2010
[cited by applicant]
WO 2012074463A1
· 2012
[cited by applicant]
WO 2012087230A1
· 2012
[cited by applicant]
Jendeberg et al., “Kinetic analysis of the interaction between protein a domain variants and human Fc using plasmon resonance detection”, Molecular Recognition, vol. 8, Issue 4, Jul./Aug. 1995, 237-279 pages., Jul./Aug.…
[cited by applicant]
Linhult et al., “Mutational Analysis of the Interaction Between Albumin-Binding Domain from Streptococcal Protein G and Human Serum Albumin”, Protein Science vol. 11, 2002, pp. 206-213.
[cited by applicant]
Ljungberg et al., “The Interaction Between Different Domains of Staphylococcal Protein A and Human Polyclonal IgG, IgA, IgM And F(ab′)2: Separation of Affinity from Specificity”, Molecular Immunology vol. 30 Number 14, …
[cited by applicant]
Ljungquist et al., “Thiol-Directed Immobilization of Recombinant IgG-Binding Receptors”, European Journal of Biochemistry vol. 186 No. 3, Dec. 22, 1989, pp. 557-561.
[cited by applicant]
Mckerrow et al., “Deamidation of Asparaginyl Residues as a Hazard an Experimental Protein and Peptide Procedures”, Department of Biology University of California, San Diego, Dec. 1, 1970, pp. 565-568.
[cited by applicant]
Mckerrow et al., “Primary Sequence Dependence of the Deamidation of Rabbit Muscle Aldolase”, Bonner Laboratory of Biology and Chemistry University of California, San Diego, Jan. 11, 1974, 1 page.
[cited by applicant]
Needleman et al., “A General Method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Proteins”, Journal of Molecular Biology vol. 48, 1970, pp. 443-453.
[cited by applicant]
Nilsson et al., “A Synthetic IgG-Binding Domain Based on Staphylococcal Protein A”, Protein Engineering vol. 1 No. 2, 1987, pp. 107-113.
[cited by applicant]
Nord et al., “Binding Proteins Selected from Combinatorial Libraries of an α-Helical Bacterial Receptor Domain”, Nature Biotechnology vol. 15, 1997, pp. 772-777.
[cited by applicant]
O'Cuinn, “Peptide Metabolism in Cytoplasm of Brain Cell”, Biochemical Society Transactions vol. 26 No. 3, 1998, pp. 279-292.
[cited by applicant]
Pace et al., “How to Measure and Predict the Molar Absorption Coefficient of a Protein”, Protein Science vol. 4, 1995, pp. 2411-2423.
[cited by applicant]
Pall,“Protein A Ceramic HyperD F—Affinity Chromatography Sorbent”, Product Note LPN PN702-004, 2004, 6 pages.
[cited by applicant]
Palmer et al., “Design of Stability at Extreme Alkaline pH in Streptococcal Protein G”, Journal of Biotechnology vol. 134, 2008, pp. 222-230.
[cited by applicant]
Patel et al., “Chemical Pathways of Peptide Degradation. II. Kinetics of Deamidation of an Asparaginyl Residue in a Model Hexapeptide”, Pharmaceutical Research vol. 7 No. 7, 1990, pp. 703-711.
[cited by applicant]
PCT/US2012/041070, “International Preliminary Report on Patentability received for PCT Application No. PCT/US2012/041070, mailed on Dec. 27, 2013”, Dec. 27, 2013, 13 pages.
[cited by applicant]
PCT/US2012/041070,“International Search Report and Written Opinion received for PCT Application No. PCT/US2012/041070, mailed on Aug. 14, 2013”, Aug. 14, 2013, 7 pages.
[cited by applicant]
Pearson et al., “Improved Tools for Biological Sequence Comparison”, Proceedings of the National Academy of Sciences vol. 85 No. 8, Apr. 1, 1988, pp. 2444-2448.
[cited by applicant]
Popplewell et al., “Synthesis and Mutagenesis of an IgG-Binding Protein based upon Protein A of
[cited by applicant]
Porath et al., “Group Fractionation of Plasma Proteins on Dipolar lon Exchangers”, Journal of Chromatography A vol. 51, 1970, pp. 479-489.
[cited by applicant]
Robinson et al., “Controlled Deamidation of Peptides and Proteins: An Experimental Hazard and a Possible Biological Timer”, Proceedings of the National Academy of Sciences vol. 66 No. 3, Jul. 1970, pp. 753-757.
[cited by applicant]
Robinson et al., “Rates of Nonenzymatic Deamidation of Glutaminyl and Asparaginyl Residues in Pentapeptides”, Journal of the American Chemical Society vol. 95 No. 24, Nov. 28, 1973, pp. 8156-8159.
[cited by applicant]
Robinson et al., “Sequence Dependent Deamidation Rates for Model Peptides of Cytochrome C”, Bonner Laboratory of Biology and Chemistry University of California at San Diego, 1974, pp. 31-35.
[cited by applicant]
Robinson et al., “Sequence Dependent Deamidation Rates for Model Peptides of Histone IV”, Linus Pauling Institute of Science and Medicine Menlo Park, 1974, pp. 279-282.
[cited by applicant]
Rodwell et al., “Structure and Functions of Proteins and Enzymes”, Amino Acids, Nov. 9, 1993, pp. 23-28.
[cited by applicant]
Roque et al., “Affinity-Based Methodologies and Ligands for Antibody Purification: Advances and Perspectives”, Journal of Chromatography A vol. 1160, 2007, pp. 44-55.
[cited by applicant]
Saito et al., “High Level Expression of a Synthetic Gene Coding for IgC-Binding Domain B of Staphylococcal Protein A”, Protein Engineering vol. 2, 1989, pp. 481-487.
[cited by applicant]
Sambrook et al., “Molecular Cloning: A Laboratory Manual”, Cold Spring Harbor Laboratory, NY, chapter 9, 1989.
[cited by applicant]
Scotchler et al., “Deamidation of Glutaminyl Residues: Dependence on pH, Temperature, and Ionic Strength”, Analytical Biochemistry vol. 59 No. 1, 1974, pp. 319-322.
[cited by applicant]
Sjodahl, “Structural Studies on the Four Repetitive Fc-Binding Regions in Protein A from
[cited by applicant]
Smith et al., “Comparison of Biosequences”, Advances in Applied Mathematics, vol. 2, No. 4, 1981, pp. 482-489.
[cited by applicant]
Starovasnik et al., “Antibody Variable Region Binding by Staphylococcal Protein A: Thermodynamic Analysis and Location of the Fv Binding Site on E-Domain”, Protein Science vol. 8 No. 7, Copyright 1999, pp. 1423-1431.
[cited by applicant]
Ulhen et al., “Complete Sequence of the Staphylococcal Gene Encoding Protein A”, A Gene Evolved Through Multiple Duplications, The Journal of Biological Chemistry vol. 259 No. 3, 1984, pp. 1695-1702.
[cited by applicant]
Yoshida et al., “Protein Having Affinity for Immunoglobulin, and Immunoglobulin-Binding Affinity Ligand”, Unpublished Japanese Patent Application No. 2009-71766, filed on Mar. 24, 2009, Corresponds to U.S. 20120208234 A…
[cited by applicant]
Mabselect Sure-Studies on Ligand Toxicity, Leakage, Removal of Leached Ligand, and Sanitization, 11-0011-64 AA, Nov. 2004, Amersham Application Note, Process-Scale Antibody Purification, Amersham Biosciences, 2004, pp. …
[cited by applicant]
Peptide Metabolism in Cytoplasm of Brain Cells, 665th Meeting, University of Southampton, Sep. 1, 1998, 1 page.
[cited by applicant]
UniProt Database Accession No. H3YRJ6, Retrieved from the Internet: URL: <http://www.uniprot.org/uniprot/H3YRJ6.txt>, Apr. 18, 2012, 1 page.
[cited by applicant]
Uniprot Database Accession No. H372S0, Retrieved from the Internet: URL: <<http:/www.uniprot.org/uniprot/H372S0.txt>, Apr. 18, 2012, 1 page.
[cited by applicant]
UniProt database accession No. Q683L6, Retrieved from the Internet: URL: <http://www.uniprot.org/uniprot/Q683L6.txt>, Oct. 11, 2004, 1 page.
[cited by applicant]
Extended European Search Report received for European Patent Application No. 012171045.3, mailed on Mar. 5, 2013, 19 pages.
[cited by applicant]
Partial European Search Report received for European Patent Application No. 012171045.3, mailed on Sep. 24, 2012, 8 pages.
[cited by applicant]
Extended European Search Report received for European Patent Application No. 09167670.0, mailed on Dec. 30, 2009, 7 pages.
[cited by applicant]
Extended European Search Report received for European Patent Application No. 09180615.8, mailed on Sep. 16, 2010, 18 pages.
[cited by applicant]
Notice of Opposition received for European Patent Application No. 09180615.8, mailed on Dec. 19, 2013, 24 pages.
[cited by applicant]
Observation filed for the European application No. 09180615.8, on Jun. 3, 2014, 17 pages.
[cited by applicant]
Partial European Search Report received for European Patent Application No. 09180615.8, mailed on May 20, 2010, 8 pages.
[cited by applicant]
Extended European Search Report received for European Patent Application No. 12163614.6, mailed on Aug. 8, 2012, 8 pages.
[cited by applicant]
Extended European Search Report received for European Patent Application No. 12163615.3, mailed on Aug. 8, 2012, 8 pages.
[cited by applicant]
Extended European Search Report received for European Patent Application No. 12171108.9, mailed on Oct. 2, 2012, 16 pages.
[cited by applicant]
Extended European Search Report received for European Patent Application No. 14163423.8, mailed on Oct. 7, 2014, 10 pages.
[cited by applicant]
Altschul et al., “Basic Local Alignment Search Tool”, Journal of Molecular Biology, vol. 215, 1990, pp. 403-410.
[cited by applicant]
Amersham Biosciences, “RMP Protein A Sepharose Fast Flow”, Data File, Affinity Chromatography, 2000, pp. 1-4.
[cited by applicant]
Arshady, “Styrene Based Polymer Supports Developed by Suspension Polymerization”, Chimica e L'Industria, vol. 70, No. 9, 1988, pp. 70-75.
[cited by applicant]
Atkins et al., “
[cited by applicant]
Ausubel et al., “Current Protocols in Molecular Biology”, Edited by Ausubel, John Wiley & Sons, 2003.
[cited by applicant]
Bowie et al., “Deciphering the Message in Protein Sequences: Tolerance to Amino Acid Substitutions”, Science vol. 247, Mar. 16, 1990, pp. 1306-1310.
[cited by applicant]
Boyle et al., “Bacterial Fc Receptors”, Nature Biotechnology, vol. 5, Jul. 1987, pp. 697-703.
[cited by applicant]
Braisted et al., “Minimizing a Binding Domain from Protein A”, Proc. Natl. Acad. Sci. USA, vol. 93, Jun. 1996, pp. 5688-5692.
[cited by applicant]
Brown et al., “A Study of the Interactions Between an IgG-Binding Domain Based on the B Domain of Staphylococcal Protein A and Rabbit IgG”, Molecular Biotechnology, vol. 10, 1998, pp. 9-16.
[cited by applicant]
Brown et al., “Affinity Purification of Human IgG using Immobilised, Mutated Immunoglobulin-Binding Domains from Protein A of
[cited by applicant]
Cedergren et al., “Mutational Analysis of the Interaction Between Staphylococcal Protein A and Human IgG”, Protein Engineering, vol. 6, 1993, pp. 441-448.
[cited by applicant]
Chen et al., “Immobilized Protein ZZ, an Affinity Tool for Immunoglobulin Isolation and Immunological Experimentation”, Biotechnology and Applied Biochemistry, vol. 45, 2006, pp. 87-92.
[cited by applicant]
Database WPI, “Week 200702”, Thomson Scientific, London GB, AN 2007-012290, XP002683879, Sep. 26, 2012, 2 pages.
[cited by applicant]
Deisenhofer, “Crystallographic Refinement and Atomic Models of a Human FC Fragment and its Complex with Fragment B of Protein A from
[cited by applicant]
Flatmark,“MMultiple Forms of Cytochrome C in the Rat”, Precursor-Product Relationship Between the Main Component Cy I and the Minor Components Cy li and Cy 3 In Vivo, Apr. 10, 1968, pp. 1623-1629.
[cited by applicant]
Flatmark,“On the Heterogeneity of Beef Heart Cytochrome C”, Acta Chemica Scandinavica, vol. 18, 1964, pp. 1656-1666.
[cited by applicant]
Füglistaller,“Comparison of Immunogloublin Binding Capacities and Ligand Leakage Using Eight Different Protein A Affinity Chromatography Matrices”, Journal of Immunological Methods, vol. 124, 1989, pp. 171-177.
[cited by applicant]
GE Healthcare, “Affinity Chromatography—Principles and Methods”, Oct. 2007, pp. 28-37.
[cited by applicant]
Geiger et al., “Deamidation, Isomerization, and Racemization at Asparaginyl and Aspartyl Residues in Peptides”, Journal of Biological Chemistry, vol. 262 No. 2, Jan. 15, 1987, pp. 785-794.
[cited by applicant]
Geneseq,“Inhibiting Complement Activation Comprises Contacting the System with a Complement-Binding Protein Comprising Sbi-III and/or Sbi-IV Domain Capable of Binding to C3 Protein”,
[cited by applicant]
Ghose et al., “Antibody Variable Region Interactions with Protein A: Implications for the Development of Generic Purification Processes”, Biotechnology and Bioengineering, vol. 92 No. 6, Dec. 20, 2005, pp. 665-673.
[cited by applicant]
Ghose et al., “Protein A Affinity Chromatography for Capture and Purification of Monoclonal Antibodies and Fc-Fusion Proteins: Practical Considerations for Process Development”, Process Scale Bioseparations for the Biop…
[cited by applicant]
Godfrey et al., “A Sensitive Enzyme-Linked Immunosorbent Assay (ELISA) for the Detection of Staphylococcal Protein A (Spa) Present as a Trace Contaminant of Murine Immunoglobulins Purified on Immobilized Protein A”, Jou…
[cited by applicant]
Graille et al., “Crystal Structure of a
[cited by applicant]
Gronberg et al., “Rapid Development of CIP Protocols for Affinity Media”, Poster Presented at the SPICA Conference, Zurich, Sep. 29-Oct. 1, 2008, 1 page.
[cited by applicant]
Gulich et al., “Protein Engineering of an IgG-Binding Domain Allows Milder Elution Conditions During Affinity Chromatography”, Journal of Biotechnology vol. 76 No. 2-3, Jan. 21, 2000,, pp. 233-243.
[cited by applicant]
Hale et al., “Repeated Cleaning of Protein A Affinity Column with Sodium Hydroxide”, Journal of Immunological Methods, vol. 171, 1994, pp. 15-21.
[cited by applicant]
Henikoff et al., “Amino Acid Substitution Matrices from Protein Blocks”, Proceedings of the National Academy of Sciences, vol. 89, Nov. 1992, p. 10915-10919.
[cited by applicant]
Hermanson et al., “Activation Methods”, Chapter 2 Affinity Ligand Techniques, Academic Press, 1992, pp. 51-136.
[cited by applicant]
Hjerten, “The Preparation of Agarose Spheres for Chromatography of Molecules and Particles”, Biochimica et Biophysica Acta vol. 79 No. 2, Mar. 30, 1964, pp. 393-398.
[cited by applicant]
Hober et al., “Protein A Chromatography for Antibody Purification”, Journal of Chromatography B, vol. 848 No. 1, Mar. 15, 2007, pp. 40-47.
[cited by applicant]
Hulett et al., “The Second and Third Extracellular Domains of Fcyri (CD64) Confer the Unique High Affinity Binding of IgG2a”, Molecular Immunology, vol. 35, 1998, pp. 989-996.
[cited by applicant]
Huston et al., “Multisite Association by Recombinant Proteins can Enhance Binding Selectivity”, Biophysical Journal vol. 62, 1992, pp. 87-91.
[cited by applicant]
Jansson et al., “All Individual Domains of Staphylococcal Protein A Show Fab Binding”, FEMS Immunology & Medical Microbiology vol. 20 No. 1, Jan. 1998, pp. 69-78.
[cited by applicant]
Office Action received for Chinese Patent Application No. 201810776217.x mailed on Jun. 15, 2022, 13 Pages (6 Pages of English translation & 7 Pages of Official Copy).
[cited by applicant]
Office Action received for Chinese Patent Application No. 201810776217.x mailing date Oct. 19, 2022, 10 Pages (5 Pages of English translation & 5 Pages of Official copy).
[cited by applicant]
Re-Examination Notification Received for Chinese Patent Application No. 201810816755.7 mailing date Oct. 27, 2022, 14 Pages (7 Pages of English Translation & 7 Pages of Official copy).
[cited by applicant]
Office Action received for Japanese Patent Application No. 2022-046955 mailing date Feb. 7, 2023, 16 Pages (8 Pages of English translation & 8 Pages of Official copy).
[cited by applicant]
Feng et al., “Biochemical Technology”, Changsha: Hunan Science and Technology Press, Nov. 30, 1989, 2 Pages.
[cited by applicant]
Ren et al., “Production Technology and Application of Biochemical Products”, Chemical Industry Press, Dec. 31, 2001, 35 Pages.
[cited by applicant]
Process Scale Bioseparations for the Biopharmaceutical Industry, CRC Press, 2006, p. 473.
[cited by applicant]
Ljungquist et al., “Immobilization and affinity purification of recombinant proteins using histidine peptide fusions”, European Journal of Biochemistry, vol. 186, Issue 3, Dec. 1989, pp. 563-569.
[cited by applicant]