• 1
    Chowdhury PS, Wu H ( 2005) Tailor-made antibody therapeutics. Methods 36: 1124.
  • 2
    Gottschalk U ( 2005) Downstream processing of monoclonal antibodies: from high dilution to high purity. Bio Pharm Int 18: 4244, 46, 48, 50, 52, 54, 56, 58.
  • 3
    Aswad, DW ( 1995) Deamidation and isoaspartate formation in peptides and proteins. Ann Arbor: CRC Press, pp 259.
  • 4
    Robinson NE, Robinson AB ( 2001) Deamidation of human proteins. Proc Natl Acad Sci USA 98: 1240912413.
  • 5
    Jenkins N, Murphy L, Tyther R ( 2008) Post-translational modifications of recombinant proteins: significance for biopharmaceuticals. Mol Biotechnol 39: 113118.
  • 6
    Robinson NE, Robinson AB ( 2001) Molecular clocks. Proc Natl Acad Sci USA 98: 944949.
  • 7
    Patel K, Borchardt RT ( 1990) Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide. Pharm Res 7: 703711.
  • 8
    Capasso S, Salvadori S ( 1999) Effect of the three-dimensional structure on the deamidation reaction of ribonuclease A. J Pept Res 54: 377382.
  • 9
    Capasso S, Di Cerbo P ( 2000) Kinetic and thermodynamic control of the relative yield of the deamidation of asparagine and isomerization of aspartic acid residues. J Pept Res 56: 382387.
  • 10
    Robinson NE, Lampi KJ, McIver RT, Williams RH, Muster WC, Kruppa G, Robinson AB ( 2005) Quantitative measurement of deamidation in lens βB2-crystallin and peptides by direct electrospray injection and fragmentation in a Fourier transform mass spectrometer. Mol Vis 11: 12111219.
  • 11
    Vlasak J, Ionescu, R (in press) Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods. Curr Pharm Biotechnol.
  • 12
    Gotte G, Libonati M, Laurents DV ( 2003) Glycosylation and specific deamidation of ribonuclease B affect the formation of three-dimensional domain-swapped oligomers. J of Biol Chem 278: 4624146251.
  • 13
    Zhang W, Czupryn MJ ( 2003) Analysis of isoaspartate in a recombinant monoclonal antibody and its charge isoforms. J Pharm Biomed Anal 30: 14791490.
  • 14
    Zabrouskov V, Han X, Welker E, Zhai H, Lin C, van Wijk KJ, Scheraga HA McLafferty FW ( 2006) Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry. Biochemistry 45: 987992.
  • 15
    Liu H, Xu B, Ray MK Shahrokh Z ( 2008) Peptide mapping with liquid chromatography using a basic mobile phase. J Chromatogr A 1210: 7683.
  • 16
    Cournoyer JJ, Pittman JL, Ivleva VB, Fallows E, Waskell L, Costello CE, O'Connor PB ( 2005) Deamidation: differentiation of aspartyl from isoaspartyl products in peptides by electron capture dissociation. Protein Sci 14: 452463.
  • 17
    Cournoyer JJ, Lin C, O'Connor PB ( 2006) Detecting deamidation products in protesin by electron capture dissociation. Anal Chem 78: 12641271.
  • 18
    Chelius D, Rehder DS, Bondarenko PV ( 2005) Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies. Anal Chem 77: 60046011.
  • 19
    Johnson BA, Shirokawa JM, Hancock WS, Spellman MW, Basa LJ Aswad DW ( 1989) Formation of isoaspartate at two distinct sites during in vitro aging of human growth hormone. J Biol Chem 264: 1426214271.
  • 20
    Stephenson RC, Clarke S ( 1989) Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J Biol Chem 264: 61646170.
  • 21
    Harris RJ, Kabakoff B, Macchi FD, Shen FJ, Kwong M, Andya JD, Shire SJ, Bjork N, Totpal K, Chen AB ( 2001) Identification of multiple sources of charge heterogeneity in a recombinant antibody. J Chromatogr B Biomed Appl 752: 233245.
  • 22
    Sadakane Y, Yamazaki T, Nakagomi K, Akizawa T, Fujii N, Tanimura T, Kaneda M, Hatanaka Y ( 2003) Quantification of the isomerization of Asp residue in recombinant human alpha A-crystallin by reversed-phase HPLC. J Pharm Biomed Anal 30: 18251833.
  • 23
    Oliyai C, Borchardt RT ( 1993) Chemical pathways of peptide degradation. IV. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide. Pharm Res 10: 95102.
  • 24
    Ren D, Ratnaswamy G, Beierle J, Treuheit MJ, Brems, DN, Bondarenko PV (in press) Degradation products analysis of an Fc fusion protein using LC/MS methods. Int J Biol Macromol.
  • 25
    Chu GC, Chelius D, Xiao G, Khor HK, Coulibaly S, Bondarenko PV ( 2007) Accumulation of succinimide in a recombinant monoclonal antibody in mildly acidic buffers under elevated temperatures. Pharm Res 24: 11451156.
  • 26
    Xiao G, Bondarenko PV, Jacob J, Chu GC, Chelius D ( 2007) 18O labeling method for identification and quantification of succinimide in proteins. Anal Chem 79: 27142721.
  • 27
    Wearne SJ, Creighton TE ( 1989) Effect of protein conformation on rate of deamidation: ribonuclease A. Proteins 5: 812.
  • 28
    Takemoto L, Fujii N, Boyle D ( 2001) Mechanism of asparagine deamidation during human senile cataractogenesis. Exp Eye Res 72: 559563.
  • 29
    Capasso S, Di Donato A, Esposito L, Sica F, Sorrentino G, Vitagliano L, Zagari A Mazzarella L ( 1996) Deamidation in proteins: the crystal structure of bovine pancreatic ribonuclease with an isoaspartyl residue at position 67. J Mol Biol 257: 492496.
  • 30
    Capasso S, Balboni G, Di Cerbo P ( 2000) Effect of lysine residues on the deamidation reaction of asparagine side chains. Biopolymers 53: 213219.
  • 31
    Capasso S, Di Cerbo P ( 2001–2000) Formation of an RNase A derivative containing an aminosuccinyl residue in place of asparagine 67. Biopolymers 56: 1419.
  • 32
    Clarke, S, Stephenson, RC, Lowenson, JD, Lability of asparagine and aspartic acid residues in proteins and peptides. In: AhernTJ, ManningMC, Eds. ( 1992) Stability of protein pharmaceuticals, part A: Chemical and physical pathways of protein degradation. New York: Plenum, pp 129.
  • 33
    Napper S, Delbaere LT, Waygood EB ( 1999) The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization. J Biol Chem 274: 2177621782.
  • 34
    Athmer L, Kindrachuk J, Georges F, Napper S ( 2002) The influence of protein structure on the products emerging from succinimide hydrolysis. J Biol Chem 277: 3050230507.
  • 35
    Ikai A, Tanford C ( 1973) Kinetics of unfolding and refolding of proteins. I. Mathematical analysis. J Mol Biol 73: 145163.
  • 36
    Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P ( 2003) Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J Mol Biol 325: 979989.