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Volumn 38, Issue 4, 2002, Pages 537-543

Study of variables involved in horseradish and soybean peroxidase purification by affinity chromatography on concanavalin A-Agarose

Author keywords

Adsorption; Chromatography; Concanavalin A Agarose; Horseradish; Peroxidase; Soybean

Indexed keywords

ARMORACIA RUSTICANA; GLYCINE MAX;

EID: 0037010795     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0032-9592(02)00166-8     Document Type: Article
Times cited : (14)

References (16)
  • 1
    • 0000805517 scopus 로고
    • On the function and mechanism of action of peroxidases
    • Dunford HB, Stillman JS. On the function and mechanism of action of peroxidases. Coordination Chem Rev 1976;19:187-251.
    • (1976) Coordination Chem Rev , vol.19 , pp. 187-251
    • Dunford, H.B.1    Stillman, J.S.2
  • 2
    • 0030876946 scopus 로고    scopus 로고
    • The N-glycosylation sites of soybean seed coat peroxidase
    • Gray JS, Montgomery R. The N-glycosylation sites of soybean seed coat peroxidase. Glycobiology 1997;7:679-85.
    • (1997) Glycobiology , vol.7 , pp. 679-685
    • Gray, J.S.1    Montgomery, R.2
  • 3
    • 0014216672 scopus 로고
    • Peroxidase isozymes from horse-radish roots
    • Kay E, Shannon LM, Lew JY. Peroxidase isozymes from horse-radish roots. J Biol Chem 1967;242:2470-3.
    • (1967) J Biol Chem , vol.242 , pp. 2470-2473
    • Kay, E.1    Shannon, L.M.2    Lew, J.Y.3
  • 4
    • 0000005531 scopus 로고
    • Purification and developmental analysis of the major anionic peroxidase from the seed coat of Glycine max
    • Gillikin JW, Graham JS. Purification and developmental analysis of the major anionic peroxidase from the seed coat of Glycine max. Plant Physiol 1991;96:214-20.
    • (1991) Plant Physiol , vol.96 , pp. 214-220
    • Gillikin, J.W.1    Graham, J.S.2
  • 5
    • 0029842169 scopus 로고    scopus 로고
    • Unusual thermal stability of soybean peroxidase
    • MacEldoon JP, Dordick JS. Unusual thermal stability of soybean peroxidase. Biotechnol Prog 1996;12:555-8.
    • (1996) Biotechnol Prog , vol.12 , pp. 555-558
    • MacEldoon, J.P.1    Dordick, J.S.2
  • 6
    • 0027561441 scopus 로고
    • Affinity-based reverse micellar extraction and separation (ARMES): A facile technique for the purification of peroxidase from soybean hulls
    • Paradkar VM, Dordick JS. Affinity-based reverse micellar extraction and separation (ARMES): A facile technique for the purification of peroxidase from soybean hulls. Biotechnol Prog 1993;9:199-203.
    • (1993) Biotechnol Prog , vol.9 , pp. 199-203
    • Paradkar, V.M.1    Dordick, J.S.2
  • 7
    • 0000194136 scopus 로고
    • Isolation and purification of horseradish peroxidase
    • Casl MT, Kostrencic C. Isolation and purification of horseradish peroxidase. Ann Clin Biochem 1987;24:271.
    • (1987) Ann Clin Biochem , vol.24 , pp. 271
    • Casl, M.T.1    Kostrencic, C.2
  • 8
    • 0001401601 scopus 로고
    • Enzymes for immunoassays
    • Burdon RH, van Knippenberg PH, editors. Amsterdam, New York, Oxford: Elsevier
    • Tijssen P. Enzymes for immunoassays. In: Burdon RH, van Knippenberg PH, editors. Practice and Theory of Enzyme Immunoassays (10). Amsterdam, New York, Oxford: Elsevier, 1985:173-220.
    • (1985) Practice and Theory of Enzyme Immunoassays (10) , pp. 173-220
    • Tijssen, P.1
  • 9
    • 0344863120 scopus 로고    scopus 로고
    • The extractive purification of peroxidase from plant raw materials in aqueous two-phase systems
    • Miranda MV, Fernández-Lahore HM, Dobrecky J, Cascone O. The extractive purification of peroxidase from plant raw materials in aqueous two-phase systems. Acta Biotechnologica 1998;18:179-88.
    • (1998) Acta Biotechnologica , vol.18 , pp. 179-188
    • Miranda, M.V.1    Fernández-Lahore, H.M.2    Dobrecky, J.3    Cascone, O.4
  • 12
    • 0021754269 scopus 로고
    • Prediction of the performance of preparative affinity chromatography
    • Chase H. Prediction of the performance of preparative affinity chromatography. J Chromatog 1984;297:179-202.
    • (1984) J Chromatog , vol.297 , pp. 179-202
    • Chase, H.1
  • 13
    • 0030042401 scopus 로고    scopus 로고
    • Structural basis of trimannoside recognition by concanavalin A
    • Naismith JH, Field RA. Structural basis of trimannoside recognition by concanavalin A. J Biol Chem 1996;271:972-6.
    • (1996) J Biol Chem , vol.271 , pp. 972-976
    • Naismith, J.H.1    Field, R.A.2
  • 14
    • 0034452750 scopus 로고    scopus 로고
    • The adsorption/desorption behaviour of horseradish peroxidase and porcine thyroglobulin on concanavalin A-Sepharose with different ligand densities
    • Franco-Fraguas L, Carlsson J, Batista-Viera F. The adsorption/desorption behaviour of horseradish peroxidase and porcine thyroglobulin on concanavalin A-Sepharose with different ligand densities. LIBC 2000;5:1-11.
    • (2000) LIBC , vol.5 , pp. 1-11
    • Franco-Fraguas, L.1    Carlsson, J.2    Batista-Viera, F.3
  • 16
    • 0031658804 scopus 로고    scopus 로고
    • Heterogeneity of glycans at each N-glycosylation site of horseradish peroxidase
    • Gray JS, Yun Yang B, Montgomery R. Heterogeneity of glycans at each N-glycosylation site of horseradish peroxidase. Carbohydrate Res 1998;311:61-9.
    • (1998) Carbohydrate Res , vol.311 , pp. 61-69
    • Gray, J.S.1    Yun Yang, B.2    Montgomery, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.