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Volumn 29, Issue 3, 1997, Pages 171-175

Hemin inhibits lipid peroxidation induced by ascorbate/FeSO4 and 2,2′-azobis-2-amidino-propane hydrochloride (ABAP)

Author keywords

Antioxidant; Hemin; Lipid peroxidation; Oxygen free radical

Indexed keywords

ALBUMIN; ANTIOXIDANT; ARACHIDONIC ACID; CYTOCHROME C; FERROUS ASCORBATE; FREE RADICAL; HEMIN; HEMOGLOBIN; HEMOPEXIN; HEMOPROTEIN; MYOGLOBIN; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID;

EID: 0030722015     PISSN: 12263613     EISSN: 20926413     Source Type: Journal    
DOI: 10.1038/emm.1997.26     Document Type: Article
Times cited : (7)

References (14)
  • 1
    • 0021322523 scopus 로고
    • Hemin-mediated oxidative degradation of proteins
    • Aft, R. L. and Mueller, G. C. (1984a) Hemin-mediated oxidative degradation of proteins. J. Biol. Chem. 259: 301-305
    • (1984) J. Biol. Chem. , vol.259 , pp. 301-305
    • Aft, R.L.1    Mueller, G.C.2
  • 2
    • 0021100151 scopus 로고
    • Hemin-mediated DNA strand scission
    • Aft, R. L. and Mueller, G. C. (1984b) Hemin-mediated DNA strand scission. J. Biol. Chem. 258: 12069-12072
    • (1984) J. Biol. Chem. , vol.258 , pp. 12069-12072
    • Aft, R.L.1    Mueller, G.C.2
  • 3
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • Ames, B. N. (1966) Assay of inorganic phosphate, total phosphate and phosphatases. Methods Enzymol. 8: 115-118
    • (1966) Methods Enzymol. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 4
    • 0024327704 scopus 로고
    • Metmyoglobin promotes arachidonic acid peroxidation at acid pH
    • Fantone, J., Jester, S. and Loomis, T. (1989) Metmyoglobin promotes arachidonic acid peroxidation at acid pH. J. Biol. Chem. 264: 9408-9411
    • (1989) J. Biol. Chem. , vol.264 , pp. 9408-9411
    • Fantone, J.1    Jester, S.2    Loomis, T.3
  • 5
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipid from animal tissue
    • Folch, J., Lees, M. and Sloane-Stanley, G. H. (1957) A simple method for the isolation and purification of total lipid from animal tissue. J. Biol. Chem. 226: 497-503
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-503
    • Folch, J.1    Lees, M.2    Sloane-Stanley, G.H.3
  • 6
    • 0024444665 scopus 로고
    • Redox cycling of myoglobin and ascorbate: A potential protective mechanism against oxidative reperfusion injury in muscle
    • Galaris, D., Cadenas, E. and Hochstein, P. (1989) Redox cycling of myoglobin and ascorbate: A potential protective mechanism against oxidative reperfusion injury in muscle. Arch. Biochem. Biophys. 272: 497-504
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 497-504
    • Galaris, D.1    Cadenas, E.2    Hochstein, P.3
  • 8
    • 0023158459 scopus 로고
    • The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation
    • Gutteridge, J. M. C. (1987) The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation. Biochim. Biophys. Acta 917: 219-223
    • (1987) Biochim. Biophys. Acta , vol.917 , pp. 219-223
    • Gutteridge, J.M.C.1
  • 9
    • 0024241523 scopus 로고
    • Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation
    • Gutteridge, J. M. C. and Smith, A. (1988) Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation. Biochem. J. 256: 861-865
    • (1988) Biochem. J. , vol.256 , pp. 861-865
    • Gutteridge, J.M.C.1    Smith, A.2
  • 10
    • 0028357330 scopus 로고
    • The effect of hemoglobin, hematin, and iron on neutrophil inactivation in Superoxide generating systems
    • Kim, Y. M., Yamazaki, I. and Piette, L. H. (1994) The effect of hemoglobin, hematin, and iron on neutrophil inactivation in Superoxide generating systems. Arch. Biochem. Biophys. 309: 308-314
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 308-314
    • Kim, Y.M.1    Yamazaki, I.2    Piette, L.H.3
  • 11
    • 0020382669 scopus 로고
    • The interaction of hemin and bilirubin with the human red cell membrane
    • Kirschner-Zilber, I., Rabizadeh, E. and Shaklai, N. (1982) The interaction of hemin and bilirubin with the human red cell membrane. Biochim. Biophys. Acta 690: 20-30
    • (1982) Biochim. Biophys. Acta , vol.690 , pp. 20-30
    • Kirschner-Zilber, I.1    Rabizadeh, E.2    Shaklai, N.3
  • 12
    • 0028919243 scopus 로고
    • Protective effects of estrogens and catecholestrogens against peroxidative membrane damage in vitro
    • Larcort, M., Leal, A. M., Liza, M., Martin, C., Marinez, R. and Ruiz-Larrea, M. B. (1995) Protective effects of estrogens and catecholestrogens against peroxidative membrane damage in vitro. Lipids 30: 141-146
    • (1995) Lipids , vol.30 , pp. 141-146
    • Larcort, M.1    Leal, A.M.2    Liza, M.3    Martin, C.4    Marinez, R.5    Ruiz-Larrea, M.B.6
  • 13
    • 0022413423 scopus 로고
    • Hemin-mediated dissociation of erythrocyte membrane skeletal proteins
    • Liu, S. C., Zhai, S., Lawler, J. and Palek, J. (1985) Hemin-mediated dissociation of erythrocyte membrane skeletal proteins. J. Biol. Chem. 260: 12234-12239
    • (1985) J. Biol. Chem. , vol.260 , pp. 12234-12239
    • Liu, S.C.1    Zhai, S.2    Lawler, J.3    Palek, J.4
  • 14
    • 0029802271 scopus 로고    scopus 로고
    • Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation
    • Miller, Y. I., Smith, A., Morgan, W. T. and Shaklai, N. (1996) Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation. Biochemistry 35: 13112-7
    • (1996) Biochemistry , vol.35 , pp. 13112-13117
    • Miller, Y.I.1    Smith, A.2    Morgan, W.T.3    Shaklai, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.