High efficiency reduction capability for the formation of Fab' antibody fragments from F(ab)2 units

Biochemistry and Biophysics Reports

Volumn 2, Issue , 2015, Pages 23-28

  Crivianu Gaita, Victor ^a   Romaschin, Alexander ^b   Thompson, Michael ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b ST MICHAEL'S HOSPITAL   (Canada)

Author keywords

Antibody reduction; Dithiobutylamine; Dithiothreitol; Fab' fragments; Mercaptoethylamine

Indexed keywords

AMINE; DITHIOBUTYLAMINE; DITHIOTHREITOL; IMMUNOGLOBULIN F(AB')2 FRAGMENT; IMMUNOGLOBULIN F(AB) FRAGMENT; MERCAPTAMINE; UNCLASSIFIED DRUG;

ANTIBODY DETECTION; ANTIGEN ANTIBODY REACTION; ARTICLE; CLONAL VARIATION; CONTROLLED STUDY; FEASIBILITY STUDY; MOLECULAR CLONING; MOLECULAR DYNAMICS; NUCLEOPHILICITY; PRIORITY JOURNAL; PROCESS OPTIMIZATION; QUALITATIVE ANALYSIS; REDUCTION KINETICS;

EID: 84937054064     PISSN: None     EISSN: 24055808     Source Type: Journal    
DOI: 10.1016/j.bbrep.2015.04.004     Document Type: Article

References (37)

1. Guzman N.A. Improved solid-phase microextraction device for use in on-line immmunoaffinity capillary electrophoresis. Electrophoresis 2003, 24:3718-3727.
2. Medina-Casanellas S., Benavente F., Barbosa J., et al. Preparation and evaluation of an immunoaffinity sorbent with Fab' antibody fragments for the analysis of opioid peptides by on-line immunoaffinity solid-phase extraction capillary electrophoresis-mass spectrometry. Anal. Chim. Acta 2013, 789:91-99.
3. Guzman N.A. Determination of immunoreactive gonadotropin-releasing hormone in serum and urine by on-line immunoaffinity capillary electrophoresis coupled to mass spectrometry. J. Chromatogr. B 2000, 749:197-213.
4. Peluso P., Wilson D.S., Do D., et al. Optimizing antibody immobilization strategies for the construction of protein microarrays. Anal. Biochem. 2003, 312:113-124.
5. Lu B., Smyth M.R., O'Kennedy R. Oriented Immobilization of Antibodies and Its Applications in Immunoassays and Immunosensors. Analyst 1996, 121:29R-32R.
6. Vikholm-Lundin I., Auer S., Hellgren A.-C. Detection of 3,4-methylenedioxymethamphetamine (MDMA, ecstasy) by displacement of antibodies. Sens. Actuator B-Chem. 2011, 156:28-34.
7. Neves-Peterson M.T., Snabe T., Klitgaard S., et al. Photonic activation of disulfide bridges achieves oriented protein immobilization on biosensor surfaces. Protein Sci. 2006, 15:343-351.
8. Clarke W., Beckwith J.D., Jackson A., et al. Antibody immobilization to high-performance liquid chromatography supports: characterization of maximum loading capacity for intact immunoglobulin G and Fab fragments. J. Chromatogr. A 2000, 888:13-22.
9. Zhao Y., Gutshall L., Jiang H., et al. Two routes for production and purification of Fab fragments in biopharmaceutical discovery research: papain digestion of mAb and transient expression in mammalian cells. Protein Exp. Purif. 2009, 67:182-189.
10. Roque A.C.A., Taipa M.A., Lowe C.R. Synthesis and screening of a rationally designed combinatorial library of affinity ligands mimicking protein L from Peptostreptococcus magnus. J. Mol. Recognit. 2005, 18:213-224.
11. Weber V., Linsberger I., Ettenauer M., et al. Development of specific adsorbents for human tumor necrosis factor-α: influence of antibody immobilization on performance and biocompatibility. Biomacromolecules 2005, 6:1864-1870.
12. Catimel B., Nerrie M., Lee F.T., et al. Kinetic analysis of the interaction between the monoclonal antibody A33 and its colonic epithelial antigen by the use of an optical biosensor: a comparison of immobilization strategies. J. Chromatogr. A 1997, 776:15-30.
13. Kumada Y., Hamasaki K., Nakagawa A. Immobilization and functional reconstitution of antibody Fab fragment by solid-phase refolding. J. Immunol. Methods 2013, 400-401:70-77.
14. Le B., Shinkai M., Kitade T. Preparation of tumor-specific magnetoliposomes and their application for hyperthermia. J. Chem. Eng. Jpn. 2001, 34:66-72.
15. Bowles M., Johnston S.C., Schoof D.D., et al. Large scale production and purification of paraquat and desipramine monoclonal antibodies and their Fab fragments, Int. J. Immunopharmac 1988, 10:537-545.
16. Helali S., Abdelghani A., Hafaiedh I., et al. Functionalization of niobium electrodes for the construction of impedimetric biosensors. Mater. Sci. Eng. C 2008, 28:826-830.
17. Adlersberg J.B. The immunoglobulin hinge (Interdomain) region. Ric Clin. Lab. 1976, 6:191-205.
18. Edmundson A.B., Guddat L.W., Andersen K.N. Crystal Structures of Intact IgG Antibodies. Immuno Methods 1993, 3:197-210.
19. Benny A.G., Lint R., Henry S.M. A simple standardized method for the preparation of pure fab fragments of rabbit immunoglobulin G. N. Z. J. Med. Lab. Technol. 1987, 41:38-39.
20. 2 fragments. J. Immunol. Methods 2002, 260:29-36.
21. 1. Mol. Immunol. 1991, 28:69-77.
22. Akita E.M., Nakai S. Production and purification of Fab[U+05F3] fragbments from chicken egg yolk immunoglobulin Y (IgY). J. Immunol. Methods 1993, 162:155-164.
23. Yamaguchi Y., Kim H., Kato K., et al. Proteolytic fragmentation with high specificity of mouse immunoglobulin G. J. Immunol. Methods 1995, 181:259-267.
24. Lukesh J.C., Palte M.J., Raines R.T. A potent, versatile disulfide-reducing agent from aspartic acid. J. Am. Chem. Soc. 2012, 134:4057-4059.
25. Cleland W.W. Dithiothreitol, a new protective reagent for SH groups. Biochemistry 1963, 3:480-482.
26. Burns J.A., Butler J.C., Moran J., et al. Selective Reduction of Disulfides by Tris(2-carboxyethyl)phosphine. J. Org. Chem. 1991, 56:2648-2650.
27. Whitesides G.M., Lilburn J.E., Szajewski R.P. Rates of thiol-disulfide interchange reactions between mono and dithiols and Ellman[U+05F3]s reagent. J. Org. Chem. 1977, 42:332-338.
28. Gray W.R. Disulfide structures of highly bridged peptides: a new strategy for analysis. Protein Sci. 1993, 2:1732-1748.
29. Cline D.J., Redding S.E., Brohawn S.G., et al. New water-soluble phosphines as reductants of peptide and protein disulfide bonds: reactivity and membrane permeability. Biochemistry 2004, 43:15195-15203.
30. Lukesh J.C., VanVeller B., Raines R.T. Thiols and selenols as electron-relay catalysts for disulfide-bond reduction. Angew. Chem. Int. Ed. 2013, 52:12901-12904.
31. a values. Biochemistry 1980, 19:4156-4166.
32. Eyer P., Worek F., Kiderlen D., et al. Molar absorption coefficients for the reduced Ellman reagent: reassessment. Anal. Biochem. 2003, 312:224-227.
33. Wolfe C.A.C., Hage D.S. Studies on the rate and control of antibody oxidation by periodate. Anal. Biochem 1995, 231:123-130.
34. Oates M.R., Clarke W., Marsh E.M., et al. Kinetic Studies on the Immobilization of antibodies to high-performance liquid chromatographic supports. Bioconjug. Chem. 1998, 9:459-465.
35. Jiskoot W., Beuvery E.C., de Koning A.A.M., et al. Analytical approaches to the study of monoclonal antibody stability. Pharm. Res. 1990, 7:1234-1241.
36. Zheng J.Y., Janis L.J. Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298. Int. J. Pharm. 2006, 308:46-51.
37. Liu H., May K. Disulfide bond structures of IgG molecules. mAbs 2012, 4:17-23.