메뉴 건너뛰기




Volumn 54, Issue 5, 2006, Pages 1584-1587

Use of soybean peroxidase in chemiluminescent enzyme-linked immunosorbent assay

Author keywords

Chemiluminescence; ELISA; Enhancement; Hydrogen peroxide; Luminol; Peroxidase; Soya

Indexed keywords

ANTIIDIOTYPIC ANTIBODY; HORSERADISH PEROXIDASE; IMMUNOGLOBULIN G; PERIODATE; PERIODIC ACID; PEROXIDASE;

EID: 33645450466     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf052643+     Document Type: Article
Times cited : (34)

References (30)
  • 1
    • 0000005531 scopus 로고
    • Purification and developmental analysis of the major anionic peroxidase from the seed coat of Glycine max
    • Gillikin, J. W.; Graham, J. S. Purification and developmental analysis of the major anionic peroxidase from the seed coat of Glycine max. Plant Physiol. 1991, 96, 214-220.
    • (1991) Plant Physiol. , vol.96 , pp. 214-220
    • Gillikin, J.W.1    Graham, J.S.2
  • 6
    • 0033121058 scopus 로고    scopus 로고
    • Recent biotechnological developments in the use of peroxidases
    • Colonna, S.; Gaggero, N.; Richelmi, C.; Pasta, P. Recent biotechnological developments in the use of peroxidases. Trends Biotechnol. 1999, 17, 163-168.
    • (1999) Trends Biotechnol. , vol.17 , pp. 163-168
    • Colonna, S.1    Gaggero, N.2    Richelmi, C.3    Pasta, P.4
  • 10
    • 0035253633 scopus 로고    scopus 로고
    • Improving the catalytical performance of peroxidases in organic synthesis
    • van de Velde, F.; van Rantwijk, F.; Sheldon, R. A. Improving the catalytical performance of peroxidases in organic synthesis. Trends Biotechnol. 2001, 19, 73-80.
    • (2001) Trends Biotechnol. , vol.19 , pp. 73-80
    • Van De Velde, F.1    Van Rantwijk, F.2    Sheldon, R.A.3
  • 12
    • 0002158301 scopus 로고    scopus 로고
    • Applications of peroxidases in modern biotechnology
    • Greppin, H., Penel, C., Broughton, W. J., Strasser, R., Eds.; University of Geneva: Geneva
    • Egorov, A. M.; Gavrilova, E. M.; Sakharov, I. Yu.Applications of peroxidases in modern biotechnology. In Integrated Plant Systems; Greppin, H., Penel, C., Broughton, W. J., Strasser, R., Eds.; University of Geneva: Geneva, 2000; pp 369-385.
    • (2000) Integrated Plant Systems , pp. 369-385
    • Egorov, A.M.1    Gavrilova, E.M.2    Sakharov, I.Yu.3
  • 14
    • 0021065776 scopus 로고
    • Enhanced luminescence procedure for sensitive determination of peroxidase-labeled conjugates in immunoassay
    • Whitehead, T. P.; Thorpe, G. H. G.; Carter, T. J. N.; Groucutt, C.; Kricka, L. J. Enhanced luminescence procedure for sensitive determination of peroxidase-labeled conjugates in immunoassay. Nature 1983, 305, 159-160.
    • (1983) Nature , vol.305 , pp. 159-160
    • Whitehead, T.P.1    Thorpe, G.H.G.2    Carter, T.J.N.3    Groucutt, C.4    Kricka, L.J.5
  • 15
    • 0030586818 scopus 로고    scopus 로고
    • Synthesis and characterization of 4-iodophenylboronic acid: A new enhancer for the horseradish peroxidase-catalyzed chemiluminescent oxidation of luminol
    • Kricka, L. J.; Cooper, M.; Ji, X. Synthesis and characterization of 4-iodophenylboronic acid: A new enhancer for the horseradish peroxidase-catalyzed chemiluminescent oxidation of luminol. Anal. Biochem. 1996, 240, 119-125.
    • (1996) Anal. Biochem. , vol.240 , pp. 119-125
    • Kricka, L.J.1    Cooper, M.2    Ji, X.3
  • 16
    • 1542613863 scopus 로고    scopus 로고
    • Employment of 4-(1-imidazoyl)-phenol as a luminol signal enhancer in a competitive-type chemiluminescence immunoassay and its comparison with the conventional antigen-horseradish peroxidase conjugate-based assay
    • Dotsikas, Y.; Loukas, Y. L. Employment of 4-(1-imidazoyl)-phenol as a luminol signal enhancer in a competitive-type chemiluminescence immunoassay and its comparison with the conventional antigen-horseradish peroxidase conjugate-based assay. Anal. Chim. Acta 2004, 509, 103-109.
    • (2004) Anal. Chim. Acta , vol.509 , pp. 103-109
    • Dotsikas, Y.1    Loukas, Y.L.2
  • 17
    • 0028838209 scopus 로고
    • Stable and general-purpose chemiluminescent detection system for horseradish peroxidase employing a thiazole compound enhancer and some additives
    • Iwata, R.; Ito, H.; Hayashi, T.; Sekine, Y.; Koyama, N.; Yamaki, M. Stable and general-purpose chemiluminescent detection system for horseradish peroxidase employing a thiazole compound enhancer and some additives. Anal. Biochem. 1995, 231, 170-174.
    • (1995) Anal. Biochem. , vol.231 , pp. 170-174
    • Iwata, R.1    Ito, H.2    Hayashi, T.3    Sekine, Y.4    Koyama, N.5    Yamaki, M.6
  • 18
    • 0031261720 scopus 로고    scopus 로고
    • Enhanced chemiluminescence reaction applied to the study of horseradish peroxidase stability in the course of p-iodophenol oxidation
    • Kapeluich, Y. L.; Rubtsova, M. Y.; Egorov, A. M. Enhanced chemiluminescence reaction applied to the study of horseradish peroxidase stability in the course of p-iodophenol oxidation. J. Biolum. Chemilum. 1997, 12, 299-308.
    • (1997) J. Biolum. Chemilum. , vol.12 , pp. 299-308
    • Kapeluich, Y.L.1    Rubtsova, M.Y.2    Egorov, A.M.3
  • 19
    • 0035324432 scopus 로고    scopus 로고
    • Long-term chemiluminescent signal is produced in the course of luminol oxidation catalyzed by peroxidase isolated from leaves of African oil palm tree
    • Sakharov, I. Yu. Long-term chemiluminescent signal is produced in the course of luminol oxidation catalyzed by peroxidase isolated from leaves of African oil palm tree. Biochemistry (Moscow) 2001, 66, 515-519.
    • (2001) Biochemistry (Moscow) , vol.66 , pp. 515-519
    • Sakharov, I.Yu.1
  • 20
    • 22544476518 scopus 로고    scopus 로고
    • Soybean peroxidase-catalyzed oxidation of luminol by hydrogen peroxide
    • Alpeeva, I. S.; Sakharov, I. Yu. Soybean peroxidase-catalyzed oxidation of luminol by hydrogen peroxide. J. Agric. Food Chem. 2005, 53, 5784-5788.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 5784-5788
    • Alpeeva, I.S.1    Sakharov, I.Yu.2
  • 21
    • 0029842169 scopus 로고    scopus 로고
    • Unusual thermal stability of soybean peroxidase
    • McEldoon, J. P.; Dordick, J. S. Unusual thermal stability of soybean peroxidase. Biotechnol. Prog. 1996, 12, 555-558.
    • (1996) Biotechnol. Prog. , vol.12 , pp. 555-558
    • McEldoon, J.P.1    Dordick, J.S.2
  • 22
    • 0037162406 scopus 로고    scopus 로고
    • Thermal and conformational stability of seed coat soybean peroxidase
    • Amisha, J. K.; Dehere, D. V. Thermal and conformational stability of seed coat soybean peroxidase. Biochemistry 2002, 41, 9034-9042.
    • (2002) Biochemistry , vol.41 , pp. 9034-9042
    • Amisha, J.K.1    Dehere, D.V.2
  • 23
    • 0037194336 scopus 로고    scopus 로고
    • Extremely high stability of African oil palm tree peroxidase
    • Sakharov, I. Yu.; Sakharova, I. V. Extremely high stability of African oil palm tree peroxidase. Biochim. Biophys. Acta 2002, 1598, 108-114.
    • (2002) Biochim. Biophys. Acta , vol.1598 , pp. 108-114
    • Sakharov, I.Yu.1    Sakharova, I.V.2
  • 26
    • 0002029484 scopus 로고
    • Recent developments in the periodate method of conjugating horseradish peroxidase (HRPO) to antibodies
    • Knapp, W., Wick, G., Eds.; Elsevier/North-Holland Medical Press: Amsterdam
    • Wilson, B. M.; Nakane, P. K. Recent developments in the periodate method of conjugating horseradish peroxidase (HRPO) to antibodies. In Immunofluorescence and Related Staining Techniques; Knapp, W., Wick, G., Eds.; Elsevier/North-Holland Medical Press: Amsterdam, 1978; pp 215-224.
    • (1978) Immunofluorescence and Related Staining Techniques , pp. 215-224
    • Wilson, B.M.1    Nakane, P.K.2
  • 27
    • 0000741089 scopus 로고
    • Soybean peroxidases: Purification and properties
    • Sessa, D. J.; Anderson, R. L. Soybean peroxidases: Purification and properties. J. Agric. Food Chem. 1981, 29, 960-965.
    • (1981) J. Agric. Food Chem. , vol.29 , pp. 960-965
    • Sessa, D.J.1    Anderson, R.L.2
  • 28
    • 0016318820 scopus 로고
    • Peroxidase-labeled antibody: A new method of conjugation
    • Nakane, P. K.; Kawaoi, A. Peroxidase-labeled antibody: A new method of conjugation. J. Histochem. Cytochem. 1974, 22, 1084-1091.
    • (1974) J. Histochem. Cytochem. , vol.22 , pp. 1084-1091
    • Nakane, P.K.1    Kawaoi, A.2
  • 29
    • 0002154654 scopus 로고
    • Horseradish peroxidase: Structure and kinetic properties
    • Everse, J., Everse, K. E., Grisham, M. B., Eds.; CRC Press: Boca Raton, FL
    • Dunford, H. B. Horseradish peroxidase: Structure and kinetic properties. In Peroxidase in Chemistry and Biology; Everse, J., Everse, K. E., Grisham, M. B., Eds.; CRC Press: Boca Raton, FL, 1991; pp 1-24.
    • (1991) Peroxidase in Chemistry and Biology , pp. 1-24
    • Dunford, H.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.