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Volumn 97, Issue 3, 2007, Pages 544-553

Determination of the origin of the N termina pyro-glutamate variation in monoclonal antibodies using model peptides

Author keywords

Bioreactor; Post translational modification; Pyro glutamate; Pyro glutamic acid; Pyro Q; Recombinant antibody

Indexed keywords

BIOREACTORS; BIOSYNTHESIS; CYCLIZATION; MONOCLONAL ANTIBODIES; ORGANIC ACIDS;

EID: 34249777508     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21260     Document Type: Article
Times cited : (108)

References (24)
  • 1
    • 0025675486 scopus 로고
    • Post-translational modification of bovine Pro-opiomelanocortin
    • Bateman A, Solomon S, Bennett HPJ. 1990. Post-translational modification of bovine Pro-opiomelanocortin. J Biol Chem 265:22130-22136.
    • (1990) J Biol Chem , vol.265 , pp. 22130-22136
    • Bateman, A.1    Solomon, S.2    Bennett, H.P.J.3
  • 5
    • 1542564130 scopus 로고
    • Application of mass spectrometry to the analysis of proteins containing a N-terminal pyroglutamic acid residue
    • deHaas GH, Franek F, Keil B, Thomas DW, Lederer E. 1969. Application of mass spectrometry to the analysis of proteins containing a N-terminal pyroglutamic acid residue. FEBS 4:25-27.
    • (1969) FEBS , vol.4 , pp. 25-27
    • deHaas, G.H.1    Franek, F.2    Keil, B.3    Thomas, D.W.4    Lederer, E.5
  • 6
    • 0000495632 scopus 로고
    • Identification of a mammalian glutaminyl cyclases converting glutaminyl into pyroglutamyl peptides
    • Fischer WH, Speiss J. 1987. Identification of a mammalian glutaminyl cyclases converting glutaminyl into pyroglutamyl peptides. PNAS 84: 3628-3632.
    • (1987) PNAS , vol.84 , pp. 3628-3632
    • Fischer, W.H.1    Speiss, J.2
  • 7
    • 33646398313 scopus 로고    scopus 로고
    • Improving mass accuracy of high performance liquid chromatography/ electrospray ionization time-of-flight mass spectrometry of intact antibodies
    • Gadgil HS, Pipes GD, Dillon TM, Treuheit MJ, Bondarenko PV. 2006. Improving mass accuracy of high performance liquid chromatography/ electrospray ionization time-of-flight mass spectrometry of intact antibodies. J Am Soc Mass Spectrom 17:867-872.
    • (2006) J Am Soc Mass Spectrom , vol.17 , pp. 867-872
    • Gadgil, H.S.1    Pipes, G.D.2    Dillon, T.M.3    Treuheit, M.J.4    Bondarenko, P.V.5
  • 9
    • 0036523742 scopus 로고    scopus 로고
    • Cyclization of N-terminal S-carbamoylmethylcysteine causing loss of 17 Da from peptides and extra peaks in peptide maps
    • Geoghegan KF, Hoth LR, Tan DH, Borzilleri KA, Withka JM, Boyd JG. 2002. Cyclization of N-terminal S-carbamoylmethylcysteine causing loss of 17 Da from peptides and extra peaks in peptide maps. J Proteom Res 1:181-187.
    • (2002) J Proteom Res , vol.1 , pp. 181-187
    • Geoghegan, K.F.1    Hoth, L.R.2    Tan, D.H.3    Borzilleri, K.A.4    Withka, J.M.5    Boyd, J.G.6
  • 11
    • 24944521480 scopus 로고    scopus 로고
    • Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation
    • Huang K, Li Y, Cheng W, Ko T, Wang AHJ. 2005. Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. PNAS 102:13117-13122.
    • (2005) PNAS , vol.102 , pp. 13117-13122
    • Huang, K.1    Li, Y.2    Cheng, W.3    Ko, T.4    Wang, A.H.J.5
  • 12
    • 0015956295 scopus 로고
    • Cell free synthesis of amino-terminal L-pyroglutamic acid
    • Jones GH. 1974. Cell free synthesis of amino-terminal L-pyroglutamic acid. Biochemistry 13:855-860.
    • (1974) Biochemistry , vol.13 , pp. 855-860
    • Jones, G.H.1
  • 13
    • 0024709472 scopus 로고
    • Influence of ions on cyclization of the amino terminal glutamine residues of tryptic peptides of streptococcal PepM49 protein
    • Khandke KM, Fairwell T, Chait BT, Manjula BN. 1989. Influence of ions on cyclization of the amino terminal glutamine residues of tryptic peptides of streptococcal PepM49 protein. Int J Peptide Protein Res 34:118-123.
    • (1989) Int J Peptide Protein Res , vol.34 , pp. 118-123
    • Khandke, K.M.1    Fairwell, T.2    Chait, B.T.3    Manjula, B.N.4
  • 14
    • 0028258349 scopus 로고
    • Characterization of humanized anti-TAC, and antibody directed against the interleukin 2 receptor, using electrospray ionization mass spectrometry by direct infusion, LC/MS, and MS/MS
    • Lewis DA, Guzzetta AW, Hancock WS, Costello M. 1994. Characterization of humanized anti-TAC, and antibody directed against the interleukin 2 receptor, using electrospray ionization mass spectrometry by direct infusion, LC/MS, and MS/MS. Anal Chem 66:585-595.
    • (1994) Anal Chem , vol.66 , pp. 585-595
    • Lewis, D.A.1    Guzzetta, A.W.2    Hancock, W.S.3    Costello, M.4
  • 15
    • 0031466912 scopus 로고    scopus 로고
    • Validation of an HPLC method for the analysis of charge heterogeneity of the recombinant monoclonal antibody IDEC-C2B8 after papain digestion
    • Moorhouse KG, Nashabeh W, Deveney J, Bjork NS, Mulkerrin MG, Ryskamp T. 1997. Validation of an HPLC method for the analysis of charge heterogeneity of the recombinant monoclonal antibody IDEC-C2B8 after papain digestion. J Pharm Biomed Anal 16:593-603.
    • (1997) J Pharm Biomed Anal , vol.16 , pp. 593-603
    • Moorhouse, K.G.1    Nashabeh, W.2    Deveney, J.3    Bjork, N.S.4    Mulkerrin, M.G.5    Ryskamp, T.6
  • 16
    • 0024473541 scopus 로고
    • Aplysia californica neurons R3-R14: Primary structure of the myoactive histidine-rich basic peptide and peptide I
    • Nagle GT, Knock SL, Painter SD, Blankenship JE, Fritz RR, Kurosk A. 1989. Aplysia californica neurons R3-R14: Primary structure of the myoactive histidine-rich basic peptide and peptide I. Peptides 10:849-857.
    • (1989) Peptides , vol.10 , pp. 849-857
    • Nagle, G.T.1    Knock, S.L.2    Painter, S.D.3    Blankenship, J.E.4    Fritz, R.R.5    Kurosk, A.6
  • 17
    • 29044447751 scopus 로고    scopus 로고
    • Reversed-phase liquid chromatography/mass spectrometry analysis of reduced monoclonal antibodies in pharmaceutics
    • Rehder DS, Dillon TM, Pipes GD, Bondarenko PV. 2006. Reversed-phase liquid chromatography/mass spectrometry analysis of reduced monoclonal antibodies in pharmaceutics. J Chrom A 1102:164-175.
    • (2006) J Chrom A , vol.1102 , pp. 164-175
    • Rehder, D.S.1    Dillon, T.M.2    Pipes, G.D.3    Bondarenko, P.V.4
  • 18
    • 1642406270 scopus 로고    scopus 로고
    • Quantitative analysis, using MALDI-TOF mass spectrometry, of the N-terminal hydrolysis and cyclization reactions of the activation process of onconase
    • Ribo M, Bosch M, Torrent G, Benito A, Beaumelle B, Vilanova M. 2004. Quantitative analysis, using MALDI-TOF mass spectrometry, of the N-terminal hydrolysis and cyclization reactions of the activation process of onconase. Eur J Biochem 271:1163-1171.
    • (2004) Eur J Biochem , vol.271 , pp. 1163-1171
    • Ribo, M.1    Bosch, M.2    Torrent, G.3    Benito, A.4    Beaumelle, B.5    Vilanova, M.6
  • 19
    • 0028787776 scopus 로고
    • An integrated strategy for structural characterization of the protein and carbohydrate components of monoclonal antibodies: Application to anti-respiratory syncytial virus mAb
    • Roberts GD, Johnson WP, Burman S, Anumala KR, Carr SA. 1995. An integrated strategy for structural characterization of the protein and carbohydrate components of monoclonal antibodies: Application to anti-respiratory syncytial virus mAb. Anal Chem 67:3613-3625.
    • (1995) Anal Chem , vol.67 , pp. 3613-3625
    • Roberts, G.D.1    Johnson, W.P.2    Burman, S.3    Anumala, K.R.4    Carr, S.A.5
  • 20
    • 0032830678 scopus 로고    scopus 로고
    • Quantitative analysis of pyroglutamic acid in peptides
    • Suzuki Y, Motoi H, Sato K. 1999. Quantitative analysis of pyroglutamic acid in peptides. J Agric Food Chem 47:3248-3251.
    • (1999) J Agric Food Chem , vol.47 , pp. 3248-3251
    • Suzuki, Y.1    Motoi, H.2    Sato, K.3
  • 21
    • 0033062814 scopus 로고    scopus 로고
    • Evidence for tissue-specific forms of glutaminyl cyclases
    • Sykes PA, Watson SJ, Temple JS, Bateman RC, Jr. 1999. Evidence for tissue-specific forms of glutaminyl cyclases. FEBS 455:159-161.
    • (1999) FEBS , vol.455 , pp. 159-161
    • Sykes, P.A.1    Watson, S.J.2    Temple, J.S.3    Bateman Jr., R.C.4
  • 22
    • 0034060128 scopus 로고    scopus 로고
    • Analysis of missed cleavage sites, tryptophan oxidation and N-terminal pyroglutamation after in-gel tryptic digestion
    • Thiede B, Lamer S, Mattow J, Siejak F, Dimmler C, Rudel T, Jungblat PR. 2000. Analysis of missed cleavage sites, tryptophan oxidation and N-terminal pyroglutamation after in-gel tryptic digestion. Rapid Commun Mass Spec 14:496-502.
    • (2000) Rapid Commun Mass Spec , vol.14 , pp. 496-502
    • Thiede, B.1    Lamer, S.2    Mattow, J.3    Siejak, F.4    Dimmler, C.5    Rudel, T.6    Jungblat, P.R.7
  • 23
    • 23844454990 scopus 로고    scopus 로고
    • Structural characterization of a recombinant monoclonal antibody by electrospray time-of-flight mass spectrometry
    • Wang L, Amphlett G, Lambert JM, Blatter W, Zhang W. 2005. Structural characterization of a recombinant monoclonal antibody by electrospray time-of-flight mass spectrometry. Pharm Res 22:1338-1349.
    • (2005) Pharm Res , vol.22 , pp. 1338-1349
    • Wang, L.1    Amphlett, G.2    Lambert, J.M.3    Blatter, W.4    Zhang, W.5
  • 24
    • 20444425289 scopus 로고    scopus 로고
    • The removal of pyroglutamic acid from monoclonal antibodies without denaturation of the protein chains
    • Werner WE, Wu S, Mulkerrin M. 2005. The removal of pyroglutamic acid from monoclonal antibodies without denaturation of the protein chains. Anal Biochem 342:120-125.
    • (2005) Anal Biochem , vol.342 , pp. 120-125
    • Werner, W.E.1    Wu, S.2    Mulkerrin, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.