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Volumn 20, Issue 3, 2004, Pages 771-776

Enantioselective affinity chromatography of a chiral drug by crystalline and carrier-bound antibody Fab fragment

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; ANTIBODIES; CROSSLINKING; CRYSTALS; ORGANIC SOLVENTS; PROTEINS;

EID: 2942746575     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp034312s     Document Type: Article
Times cited : (10)

References (29)
  • 1
    • 0035847272 scopus 로고    scopus 로고
    • Separation of enantiomers: Needs, challenges, perspectives
    • Maier, N. M.; Franco, P.; Lindner, W. Separation of enantiomers: needs, challenges, perspectives. J. Chromatogr., A 2001, 906, 3-33.
    • (2001) J. Chromatogr., A , vol.906 , pp. 3-33
    • Maier, N.M.1    Franco, P.2    Lindner, W.3
  • 2
    • 0043072352 scopus 로고    scopus 로고
    • The impact of chiral technology on the pharmaceutical industry
    • 2 June
    • Richards, A.; McCague, R. The impact of chiral technology on the pharmaceutical industry. Chem. Ind. (London) 1997, 2 June, 422-425.
    • (1997) Chem. Ind. (London) , pp. 422-425
    • Richards, A.1    McCague, R.2
  • 3
    • 0035847245 scopus 로고    scopus 로고
    • Protein-based chiral statinary phases for high-performance liquid chromatography enantioseparations
    • Haginaka, J. Protein-based chiral statinary phases for high-performance liquid chromatography enantioseparations. J. Chromatogr., A 2001, 906, 253-273.
    • (2001) J. Chromatogr., A , vol.906 , pp. 253-273
    • Haginaka, J.1
  • 4
    • 9944250646 scopus 로고
    • Synthesis and chromatographic properties of an HPLC chiral stationary phase based upon human serum albumin
    • Domenici, E.; Bertucci, C.; Salvadori, P.; Felix, G.; Cahagne, I.; Motellier, S.; Wainer, I. W. Synthesis and chromatographic properties of an HPLC chiral stationary phase based upon human serum albumin. Chromatographia 1990, 29, 170-176.
    • (1990) Chromatographia , vol.29 , pp. 170-176
    • Domenici, E.1    Bertucci, C.2    Salvadori, P.3    Felix, G.4    Cahagne, I.5    Motellier, S.6    Wainer, I.W.7
  • 5
    • 0021647715 scopus 로고
    • Direct liquid chromatographic separation of enantiomers on immobilized protein stationary phases. IV. Molecular interaction forces and retention behaviour in chromatography on bovine serum albumin as a stationary phase
    • Allenmark, S.; Bomgren, B.; Boren, H. Direct liquid chromatographic separation of enantiomers on immobilized protein stationary phases. IV. Molecular interaction forces and retention behaviour in chromatography on bovine serum albumin as a stationary phase. J. Chromatogr. 1984, 316, 617-624.
    • (1984) J. Chromatogr. , vol.316 , pp. 617-624
    • Allenmark, S.1    Bomgren, B.2    Boren, H.3
  • 6
    • 0021090901 scopus 로고
    • Direct liquid chromatographic resolution of racemic drugs using α1-acid glycoprotein as the chiral stationary phase
    • Hermansson, J. Direct liquid chromatographic resolution of racemic drugs using α1-acid glycoprotein as the chiral stationary phase. J. Chromatogr. 1983, 269, 71-80.
    • (1983) J. Chromatogr. , vol.269 , pp. 71-80
    • Hermansson, J.1
  • 7
    • 0000799144 scopus 로고
    • Immobilized cellulase (CBH I) as a chiral stationary phase for direct resolution of enantiomers
    • Erlandsson, P.; Marie, I.; Hansson, L.; Isaksson, R.; Pettersson, G.; Pettersson, C. Immobilized cellulase (CBH I) as a chiral stationary phase for direct resolution of enantiomers. J. Am. Chem. Soc. 1990, 112, 4573-4574.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4573-4574
    • Erlandsson, P.1    Marie, I.2    Hansson, L.3    Isaksson, R.4    Pettersson, G.5    Pettersson, C.6
  • 8
    • 0028348275 scopus 로고
    • Separation of enantiomers on a lysozyme-bonded silica column
    • Haginaka, J.; Murashima, T.; Seyama, C. Separation of enantiomers on a lysozyme-bonded silica column. J. Chromatogr., A 1994, 666, 203-210.
    • (1994) J. Chromatogr., A , vol.666 , pp. 203-210
    • Haginaka, J.1    Murashima, T.2    Seyama, C.3
  • 9
    • 34249969003 scopus 로고
    • Immobilized enzymes as chromatographic phases for HPLC: The chromatography of free and derivatized amino acids on immobilized trypsin
    • Thelohan, S.; Jadaud, P.; Wainer, I. W. Immobilized enzymes as chromatographic phases for HPLC: the chromatography of free and derivatized amino acids on immobilized trypsin. Chromatographia 1989, 28, 551-555.
    • (1989) Chromatographia , vol.28 , pp. 551-555
    • Thelohan, S.1    Jadaud, P.2    Wainer, I.W.3
  • 10
    • 0034031370 scopus 로고    scopus 로고
    • Cross-linked glucose isomerase crystals as a liquid chromatographic separation material
    • Pastinen, O.; Jokela, J.; Eerikäinen, T.; Schwabe, T.; Leisola, M. Cross-linked glucose isomerase crystals as a liquid chromatographic separation material. Enzyme Microb. Technol. 2000, 26, 550-558.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 550-558
    • Pastinen, O.1    Jokela, J.2    Eerikäinen, T.3    Schwabe, T.4    Leisola, M.5
  • 13
    • 0031810912 scopus 로고    scopus 로고
    • Fine-tuning of an anti-testosterone antibody binding site by stepwise optimization of the CDRs
    • Hemminki, A.; Niemi, S.; Hautoniemi, L.; Söderlund, H.; Takkinen, K. Fine-tuning of an anti-testosterone antibody binding site by stepwise optimization of the CDRs. Immunotechnology 1998, 4, 59-69.
    • (1998) Immunotechnology , vol.4 , pp. 59-69
    • Hemminki, A.1    Niemi, S.2    Hautoniemi, L.3    Söderlund, H.4    Takkinen, K.5
  • 15
    • 1442359486 scopus 로고    scopus 로고
    • Model based mutagenesis to improve the enantioselective fractionation properties of an antibody
    • submitted for publication
    • Nevanen, T. K.; Hellman, M.-L.; Munck, N.; Wohlfahrt, G.; Koivula, A.; Söderlund, H. Model based mutagenesis to improve the enantioselective fractionation properties of an antibody. Prot. Eng. 2003, submitted for publication.
    • (2003) Prot. Eng.
    • Nevanen, T.K.1    Hellman, M.-L.2    Munck, N.3    Wohlfahrt, G.4    Koivula, A.5    Söderlund, H.6
  • 17
    • 0029060763 scopus 로고
    • Cross-linked crystals of Candida rugosa lipase: Highly efficient catalysts for the resolution of chiral esters
    • Lalonde, J. J.; Govardhan, C.; Khalaf, N.; Martinez, A. G.; Visuri, K.; Margolin, A. L. Cross-linked crystals of Candida rugosa lipase: highly efficient catalysts for the resolution of chiral esters. J. Am. Chem. Soc. 1995, 117, 6845-6852.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6845-6852
    • Lalonde, J.J.1    Govardhan, C.2    Khalaf, N.3    Martinez, A.G.4    Visuri, K.5    Margolin, A.L.6
  • 18
    • 0035907697 scopus 로고    scopus 로고
    • Protein crystals as novel catalytic materials
    • Margolin, A. L.; Navia, M. A. Protein crystals as novel catalytic materials. Angew. Chem., Int. Ed. 2001, 40, 2204-2222.
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 2204-2222
    • Margolin, A.L.1    Navia, M.A.2
  • 19
    • 0033179495 scopus 로고    scopus 로고
    • Cross-linking of enzymes for improved stability and performance
    • Govardhan, C. P. Cross-linking of enzymes for improved stability and performance. Curr. Opin. Biotechnol. 1999, 10, 331-335.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 331-335
    • Govardhan, C.P.1
  • 21
    • 0141627911 scopus 로고    scopus 로고
    • Development of cross-linked antibody Fab fragment crystals for enantioselective separation of a drug enantiomer
    • Vuolanto, A.; Kiviharju, K.; Nevanen, T. K.; Leisola, M.; Jokela, J. Development of cross-linked antibody Fab fragment crystals for enantioselective separation of a drug enantiomer. Cryst. Growth Des. 2003, 3, 777-782.
    • (2003) Cryst. Growth Des. , vol.3 , pp. 777-782
    • Vuolanto, A.1    Kiviharju, K.2    Nevanen, T.K.3    Leisola, M.4    Jokela, J.5
  • 23
  • 24
    • 0035916376 scopus 로고    scopus 로고
    • Simultaneous catalysis and product separation by cross-linked enzyme crystals
    • Leisola, M.; Jokela, J.; Finell, J.; Pastinen, O. Simultaneous catalysis and product separation by cross-linked enzyme crystals. Biotechnol. Bioeng. 2001, 72, 501-505.
    • (2001) Biotechnol. Bioeng. , vol.72 , pp. 501-505
    • Leisola, M.1    Jokela, J.2    Finell, J.3    Pastinen, O.4
  • 25
    • 0036092233 scopus 로고    scopus 로고
    • Total hydrolysis of xylotetraose and xylobiose by soluble and cross-linked crystalline xylanase II from Trichoderma reesei
    • Finell, J.; Jokela, J.; Leisola, M.; Riekkola, M.-L. Total hydrolysis of xylotetraose and xylobiose by soluble and cross-linked crystalline xylanase II from Trichoderma reesei. Biocatal. Biotrans. 2002, 20, 281-290.
    • (2002) Biocatal. Biotrans. , vol.20 , pp. 281-290
    • Finell, J.1    Jokela, J.2    Leisola, M.3    Riekkola, M.-L.4
  • 26
    • 0026595584 scopus 로고
    • Retention of racemic solutes on a modified ovomucoid-bonded column
    • Haginaka, J.; Seyama, C.; Yasuda, H. Retention of racemic solutes on a modified ovomucoid-bonded column. J. Chromatogr. 1992, 592, 301-307.
    • (1992) J. Chromatogr. , vol.592 , pp. 301-307
    • Haginaka, J.1    Seyama, C.2    Yasuda, H.3
  • 28
    • 0018830522 scopus 로고
    • Stabilization of proteins immobilized on sepharose from leakage by glutaraldehyde cross-linking
    • Kowal, R.; Parsons, R. G. Stabilization of proteins immobilized on sepharose from leakage by glutaraldehyde cross-linking. Anal. Biochem. 1980, 102, 72-76.
    • (1980) Anal. Biochem. , vol.102 , pp. 72-76
    • Kowal, R.1    Parsons, R.G.2
  • 29
    • 0024514490 scopus 로고
    • Stabilization of immobilized lectin column by cross-linking with glutaraldehyde
    • Scher, M. G.; Resneck, W. G.; Bloch, R. J. Stabilization of immobilized lectin column by cross-linking with glutaraldehyde. Anal. Biochem. 1989, 177, 168-171.
    • (1989) Anal. Biochem. , vol.177 , pp. 168-171
    • Scher, M.G.1    Resneck, W.G.2    Bloch, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.