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Volumn 32, Issue 8, 2005, Pages 794-799

Micropreparation of a native PHGPx protein from radish seedlings by immunoaffinity chromatography

Author keywords

Immunoaffinity chromatography; Native protein; Phospholipid hydroperoxide glutathione peroxidase; Polyclonal antibodies; Radish

Indexed keywords

ORYCTOLAGUS CUNICULUS; RAPHANUS SATIVUS;

EID: 27744538987     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (24)
  • 2
    • 0037438730 scopus 로고    scopus 로고
    • Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells
    • Imai H, Nakagawa Y. Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic Bio Med, 2003, 34 (2): 145-169
    • (2003) Free Radic Bio Med , vol.34 , Issue.2 , pp. 145-169
    • Imai, H.1    Nakagawa, Y.2
  • 3
    • 0029063167 scopus 로고
    • A stress-associated citrus protein is a distinct plant phospholipid hydroperoxide glutathione peroxidase
    • Beeor-Tzahar T, Ben-Hayyim G, Holland D, et al. A stress-associated citrus protein is a distinct plant phospholipid hydroperoxide glutathione peroxidase. FEBS Lett, 1995, 366 (1-2): 151-155
    • (1995) FEBS Lett , vol.366 , Issue.1-2 , pp. 151-155
    • Beeor-Tzahar, T.1    Ben-Hayyim, G.2    Holland, D.3
  • 4
    • 0030908451 scopus 로고    scopus 로고
    • Plant glutathione peroxidases
    • Eshdat Y, Holland D, Faltin Z, et al. Plant glutathione peroxidases. Physiol Plant, 1997, 100 (2): 234-240
    • (1997) Physiol Plant , vol.100 , Issue.2 , pp. 234-240
    • Eshdat, Y.1    Holland, D.2    Faltin, Z.3
  • 6
    • 0027562881 scopus 로고
    • Molecular characterization of salt stress-associated protein in citrus: Protein and cDNA sequence homology to mammalian glutathione peroxidases
    • Holland D, Ben-Hayyim G, Faltin Z, et al. Molecular characterization of salt stress-associated protein in citrus: protein and cDNA sequence homology to mammalian glutathione peroxidases, Plant Mol Biol, 1993, 21 (5): 923-927
    • (1993) Plant Mol Biol , vol.21 , Issue.5 , pp. 923-927
    • Holland, D.1    Ben-Hayyim, G.2    Faltin, Z.3
  • 7
    • 0032005969 scopus 로고    scopus 로고
    • Identification of cDNAs encoding plastid-targeted glutathione peroxidase
    • Mullineaux P M, Karpinski S, Jimenez A, et al. Identification of cDNAs encoding plastid-targeted glutathione peroxidase. Plant J, 1998, 13 (3): 375-379
    • (1998) Plant J , vol.13 , Issue.3 , pp. 375-379
    • Mullineaux, P.M.1    Karpinski, S.2    Jimenez, A.3
  • 8
    • 0032871989 scopus 로고    scopus 로고
    • A gene family encoding glutathione peroxidase homologues in Hordeum vulgare (barley)
    • Churin Y, Schilling S, Borner T. A gene family encoding glutathione peroxidase homologues in Hordeum vulgare (barley). FEBS Lett, 1999, 459 (1): 33-38
    • (1999) FEBS Lett , vol.459 , Issue.1 , pp. 33-38
    • Churin, Y.1    Schilling, S.2    Borner, T.3
  • 9
    • 0034618524 scopus 로고    scopus 로고
    • Molecular cloning and expression of a phospholipid hydroperoxide glutathione peroxidase homolog in Oryza sativa
    • Li W J, Feng H, Fan J H, et al. Molecular cloning and expression of a phospholipid hydroperoxide glutathione peroxidase homolog in Oryza sativa. Biochim Biophys Acta, 2000, 1493 (2): 225-230
    • (2000) Biochim Biophys Acta , vol.1493 , Issue.2 , pp. 225-230
    • Li, W.J.1    Feng, H.2    Fan, J.H.3
  • 11
    • 3543022743 scopus 로고    scopus 로고
    • Tomato phospholipid hydroperoxide glutathione peroxidase inhibits cell death induced by bax and oxidative stresses in yeast and plants
    • Chen S, Vaghchhipawala Z, Li W, et al. Tomato phospholipid hydroperoxide glutathione peroxidase inhibits cell death induced by bax and oxidative stresses in yeast and plants. Plant Physiol, 2004, 135 (3): 1630-1641
    • (2004) Plant Physiol , vol.135 , Issue.3 , pp. 1630-1641
    • Chen, S.1    Vaghchhipawala, Z.2    Li, W.3
  • 12
    • 27744452792 scopus 로고    scopus 로고
    • Cloning and initial characterization of a rasPHGPX, a Raphanus sativus homolog of mammalian PHGPXs
    • Liu J, Li W, Yang X, et al. Cloning and initial characterization of a rasPHGPX, a Raphanus sativus homolog of mammalian PHGPXs. Plant Cell Physiol, 2002, 43 (Supp): 197
    • (2002) Plant Cell Physiol , vol.43 , Issue.SUPPL. , pp. 197
    • Liu, J.1    Li, W.2    Yang, X.3
  • 13
    • 18044363128 scopus 로고    scopus 로고
    • Isolation and characterization of a novel PHGPx gene in Raphanus sativus
    • Yang X D, Li W J, Liu J Y. Isolation and characterization of a novel PHGPx gene in Raphanus sativus. Biochim Biophys Acta, 2005, 1728 (3): 199-205
    • (2005) Biochim Biophys Acta , vol.1728 , Issue.3 , pp. 199-205
    • Yang, X.D.1    Li, W.J.2    Liu, J.Y.3
  • 14
    • 0032055781 scopus 로고    scopus 로고
    • Mitochondrial targeting peptides in plants
    • Sjöling S, Glaser E. Mitochondrial targeting peptides in plants. Trends Plant Sci, 1998, 3 (4): 136-140
    • (1998) Trends Plant Sci , vol.3 , Issue.4 , pp. 136-140
    • Sjöling, S.1    Glaser, E.2
  • 15
    • 0037204853 scopus 로고    scopus 로고
    • Purification of antibodies by affinity chromatography
    • Huse K, Bohme H J, Scholz G H. Purification of antibodies by affinity chromatography. J Biochem Biophys Methods, 2002, 51 (3): 217-231
    • (2002) J Biochem Biophys Methods , vol.51 , Issue.3 , pp. 217-231
    • Huse, K.1    Bohme, H.J.2    Scholz, G.H.3
  • 16
    • 0032508563 scopus 로고    scopus 로고
    • Survey of recent advances in analytical applications of immunoaffinity chromatography
    • Hage D S. Survey of recent advances in analytical applications of immunoaffinity chromatography. J Chromatogr B, 1998, 715 (1): 3-28
    • (1998) J Chromatogr B , vol.715 , Issue.1 , pp. 3-28
    • Hage, D.S.1
  • 17
    • 0023098437 scopus 로고
    • Immunoaffinity chromatography utilizingmonoclonal antibodies. Factors which influence antigen-binding capacity
    • Pfeiffer N E, Wylier D E, Schuster S M. Immunoaffinity chromatography utilizingmonoclonal antibodies. Factors which influence antigen-binding capacity. J Immunol Methods, 1987, 97 (1): 1-9
    • (1987) J Immunol Methods , vol.97 , Issue.1 , pp. 1-9
    • Pfeiffer, N.E.1    Wylier, D.E.2    Schuster, S.M.3
  • 19
    • 0021297276 scopus 로고
    • Immunosorbent separations
    • Calton G J. Immunosorbent separations. Methods Enzymol, 1984, 104: 381-387
    • (1984) Methods Enzymol , vol.104 , pp. 381-387
    • Calton, G.J.1
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micro quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of micro quantities of protein utilizing the principle of protein-dye binding. Anal Biochem, 1976, 72 (1-2): 248-254
    • (1976) Anal Biochem , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.1
  • 21
    • 0347947728 scopus 로고    scopus 로고
    • Affinity purification of immunoglobulins from chicken egg yolk using a new synthetic ligand
    • Verdoliva A, Basile G, Fassina G. Affinity purification of immunoglobulins from chicken egg yolk using a new synthetic ligand. J Chromatogr B, 2002, 749 (2): 233-242
    • (2002) J Chromatogr B , vol.749 , Issue.2 , pp. 233-242
    • Verdoliva, A.1    Basile, G.2    Fassina, G.3
  • 22
    • 0033729605 scopus 로고    scopus 로고
    • Mitochondrial localization of AtOXA1, an Arabidopsis homologue of yeast Oxa1p involved in the insertion and assembly of protein complexes in mitochondrial inner membrane
    • Sakamoto W, Spielewoy N, Bonnard G, et al. Mitochondrial localization of AtOXA1, an Arabidopsis homologue of yeast Oxa1p involved in the insertion and assembly of protein complexes in mitochondrial inner membrane. Plant Cell Physiol, 2000, 41 (10): 1157-1163
    • (2000) Plant Cell Physiol , vol.41 , Issue.10 , pp. 1157-1163
    • Sakamoto, W.1    Spielewoy, N.2    Bonnard, G.3
  • 23
    • 0032750685 scopus 로고    scopus 로고
    • Production and characterization of polyclonal antibodies to sulfamethazine and their potential use in immunoaffinity chromatography for urine sample pre-treatment
    • Crabbe P, Haasnoot W, Kohen F, et al. Production and characterization of polyclonal antibodies to sulfamethazine and their potential use in immunoaffinity chromatography for urine sample pre-treatment. Analyst, 1999, 124 (11): 1569-1575
    • (1999) Analyst , vol.124 , Issue.11 , pp. 1569-1575
    • Crabbe, P.1    Haasnoot, W.2    Kohen, F.3
  • 24
    • 0036437313 scopus 로고    scopus 로고
    • Immunoglobulin purification by affinity chromatography using protein A mimetic ligands prepared by combinatorial chemical synthesis
    • Kabir S. Immunoglobulin purification by affinity chromatography using protein A mimetic ligands prepared by combinatorial chemical synthesis. Immunol Invest, 2002, 31 (3-4): 263-278
    • (2002) Immunol Invest , vol.31 , Issue.3-4 , pp. 263-278
    • Kabir, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.