Studies in serum support rapid formation of disulfide bond between unpaired cysteine residues in the VH domain of an immunoglobulin G1 molecule

Analytical Biochemistry

Volumn 397, Issue 1, 2010, Pages 37-47

  Ouellette, D ^a   Alessandri, L ^a   Chin, A ^a   Grinnell, C ^a   Tarcsa, E ^a   Radziejewski, C ^a   Correia, I ^a  

^a ABBOTT LABORATORIES   (United States)

Author keywords

Antibody; IgG1; Mass spectrometry; Protein; Unpaired cysteines; Weak cation exchange chromatography

Indexed keywords

ANTIBODIES; CHROMATOGRAPHY; COVALENT BONDS; MASS SPECTROMETRY; MOLECULES; MONOCLONAL ANTIBODIES; POSITIVE IONS; PROTEINS; SULFUR COMPOUNDS;

ANALYTICAL EVALUATION; CATION EXCHANGE CHROMATOGRAPHY; IGG1; MONOCLONAL ANTIBODIES (MAB); POST-TRANSLATIONAL MODIFICATIONS; RECOMBINANT MONOCLONAL ANTIBODY; UNPAIRED CYSTEINES; WEAK CATION EXCHANGE CHROMATOGRAPHY;

AMINO ACIDS;

CYSTEINE; DISULFIDE; GLUTATHIONE; HOMOCYSTEINE; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; ISOPROTEIN; MONOCLONAL ANTIBODY; OMALIZUMAB; PYROGLUTAMIC ACID; THIOL;

AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; CYCLIZATION; DISULFIDE BOND; ENDOPLASMIC RETICULUM; ION EXCHANGE CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RAT; SERUM;

EID: 71749117526     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.09.027     Document Type: Article

References (19)

1. Chirino A.J., and Mire-Sluis A. Characterizing biological products and assessing comparability following manufacturing changes. Nat. Biotechnol. 22 (2004) 1383-1391
2. Chirino A.J., and Mire-Sluis A.R. State of the art analytical comparability: a review. Dev. Biol. (Basel) 122 (2005) 3-26
3. Weitzhandler M., Farnan D., Rohrer J.S., and Avdalovic N. Protein variant separations using cation exchange chromatography on grafted, polymeric stationary phases. Proteomics 1 (2001) 179-185
4. Johnson K.A., Paisley-Flango K., Tangarone B.S., Porter T.J., and Rouse J.C. Cation exchange - HPLC and mass spectrometry reveal C-terminal amidation of an IgG1 heavy chain. Anal. Biochem. 360 (2007) 75-83
5. Jessop C.E., Chakravarthi S., Watkins R.H., and Bulleid N.J. Oxidative protein folding in the mammalian endoplasmic reticulum. Biochem. Soc. Trans. 32 (2004) 655-658
6. Frand A.R., Cuozzo J.W., and Kaiser C.A. Pathways for protein disulphide bond formation. Trends Cell Biol. 10 (2000) 203-210
7. Gevondyan N.M., Volynskaia A.M., and Gevondyan V.S. Four free cysteine residues found in human IgG1 of healthy donors. Biochemistry (Mosc.) 71 (2006) 279-284
8. Chaderjian W.B., Chin E.T., Harris R.J., and Etcheverry T.M. Effect of copper sulfate on performance of a serum-free CHO cell culture process and the level of free thiol in the recombinant antibody expressed. Biotechnol. Prog. 21 (2005) 550-553
9. Liu Y.D., Chen X., Enk J.Z., Plant M., Dillon T.M., and Flynn G.C. Human IgG2 antibody disulfide rearrangement in vivo. J. Biol. Chem. 283 (2008) 29266-29272
10. Dillon T.M., Ricci M.S., Vezina C., Flynn G.C., Liu Y.D., Rehder D.S., Plant M., Henkle B., Li Y., Deechongkit S., Varnum B., Wypych J., Balland A., and Bondarenko P.V. Structural and functional characterization of disulfide isoforms of the human IgG2 subclass. J. Biol. Chem. 283 (2008) 16206-16215
11. Wypych J., Li M., Guo A., Zhang Z., Martinez T., Allen M.J., Fodor S., Kelner D.N., Flynn G.C., Liu Y.D., Bondarenko P.V., Ricci M.S., Dillon T.M., and Balland A. Human IgG2 antibodies display disulfide-mediated structural isoforms. J. Biol. Chem. 283 (2008) 16194-16205
12. Zhang Z., and Henzel W.J. Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 13 (2004) 2819-2824
13. Chelius D., Jing K., Lueras A., Rehder D.S., Dillon T.M., Vizel A., Rajan R.S., Li T., Treuheit M.J., and Bondarenko P.V. Formation of pyroglutamic acid from N-terminal glutamic acid in immunoglobulin gamma antibodies. Anal. Chem. 78 (2006) 2370-2376
14. Rehder D.S., Dillon T.M., Pipes G.D., and Bondarenko P.V. Reversed-phase liquid chromatography/mass spectrometry analysis of reduced monoclonal antibodies in pharmaceutics. J. Chromatogr. A 1102 (2006) 164-175
15. Abraham G.N., and Podell D.N. Pyroglutamic acid: non-metabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal. Mol. Cell. Biochem. 38 (1981) 181-190
16. Podell D.N., and Abraham G.N. A technique for the removal of pyroglutamic acid from the amino terminus of proteins using calf liver pyroglutamate amino peptidase. Biochem. Biophys. Res. Commun. 81 (1978) 176-185
17. Harris R.J. Heterogeneity of recombinant antibodies: linking structure to function. Dev. Biol. (Basel) 122 (2005) 117-127
18. Summa D., Spiga O., Bernini A., Venditti V., Priora R., Frosali S., Margaritis A., Di Giuseppe D., Niccolai N., and Di Simplicio P. Protein-thiol substitution or protein dethiolation by thiol/disulfide exchange reactions: the albumin model. Proteins 69 (2007) 369-378
19. Di Giuseppe D., Di Simplicio P., Capecchi P.L., Lazzerini P.E., and Pasini F.L. Alteration in the redox state of plasma in heart-transplant patients with moderate hyperhomocysteinemia. J. Lab. Clin. Med. 142 (2003) 21-28