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Volumn 52, Issue 6, 1996, Pages 927-931

Kinetics of aluminum-induced inhibition of δ-aminolevulinic acid dehydratase in vitro

Author keywords

aluminum inhibition; heme biosynthesis; porphobilinogen synthetase; porphyrins; aminolevulinic acid dehydratase

Indexed keywords

ALUMINUM CHLORIDE; CITRIC ACID; ERYTHROCYTE ENZYME; HEME; LIVER ENZYME; PORPHOBILINOGEN SYNTHASE;

EID: 0030603966     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-2952(96)00449-2     Document Type: Article
Times cited : (16)

References (26)
  • 1
    • 0018581777 scopus 로고
    • Purification and properties of δ-aminolevulinic acid dehydratase from human erythrocytes
    • 1. Anderson PM and Desnick RJ, Purification and properties of δ-aminolevulinic acid dehydratase from human erythrocytes. J Biol Chem 254: 6924-6930, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 6924-6930
    • Anderson, P.M.1    Desnick, R.J.2
  • 2
    • 0018788882 scopus 로고
    • The role of zinc with special reference to the essential thiol groups in δ-aminolevulinic acid dehydratase of bovine liver
    • 2. Tsukamoto I, Yoshinaga T and Sano S, The role of zinc with special reference to the essential thiol groups in δ-aminolevulinic acid dehydratase of bovine liver. Biochim Biophvs Acta 570: 167-178, 1979.
    • (1979) Biochim Biophvs Acta , vol.570 , pp. 167-178
    • Tsukamoto, I.1    Yoshinaga, T.2    Sano, S.3
  • 3
    • 0019320820 scopus 로고
    • Mechanism of porphobilinogen synthase
    • 3. Bevan DR, Bodlaender P and Shemin D, Mechanism of porphobilinogen synthase. J Biol Chem 255:2030-2035, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 2030-2035
    • Bevan, D.R.1    Bodlaender, P.2    Shemin, D.3
  • 4
    • 0011782611 scopus 로고
    • Azione di alcuni metalli sull'ALA-deidratase eritrocitaria purificata da sangue umano
    • 4. Calissano P, Cartasegna C and Bonsignore D, Azione di alcuni metalli sull'ALA-deidratase eritrocitaria purificata da sangue umano. Lav Um 17: 493-497, 1965.
    • (1965) Lav Um , vol.17 , pp. 493-497
    • Calissano, P.1    Cartasegna, C.2    Bonsignore, D.3
  • 5
    • 77049239695 scopus 로고
    • The purification and properties of δ-aminolevulinic acid dehydratase
    • 5. Gibson KD, Neuberger A and Scott JJ, The purification and properties of δ-aminolevulinic acid dehydratase. Biochem J 61: 618-629, 1955.
    • (1955) Biochem J , vol.61 , pp. 618-629
    • Gibson, K.D.1    Neuberger, A.2    Scott, J.J.3
  • 6
    • 0014291103 scopus 로고
    • Effect of lead exposure on the level of δ-aminolevulinic dehydratase activity
    • 6. DeBruin A, Effect of lead exposure on the level of δ-aminolevulinic dehydratase activity. Med Lav 59: 411-418, 1968.
    • (1968) Med Lav , vol.59 , pp. 411-418
    • DeBruin, A.1
  • 7
    • 0018973161 scopus 로고
    • Correlation of the physicochemical properties of metal ions with their activation and inhibition of human erythrocytic δ-aminolevulinic acid dehydratase (ALAD) in vitro
    • 7. Davis JR and Avram MJ, Correlation of the physicochemical properties of metal ions with their activation and inhibition of human erythrocytic δ-aminolevulinic acid dehydratase (ALAD) in vitro. Toxicol Appl Pharmacol 55: 281-290, 1980.
    • (1980) Toxicol Appl Pharmacol , vol.55 , pp. 281-290
    • Davis, J.R.1    Avram, M.J.2
  • 8
    • 0014250146 scopus 로고
    • δ-Aminolevulinic acid dehydratase activity in erythrocytes for the evaluation of lead poisoning
    • 8. Nakao K, Wada O and Yano Y, δ-Aminolevulinic acid dehydratase activity in erythrocytes for the evaluation of lead poisoning. Clin Chim Acta 19: 319-325, 1968.
    • (1968) Clin Chim Acta , vol.19 , pp. 319-325
    • Nakao, K.1    Wada, O.2    Yano, Y.3
  • 9
    • 0011782612 scopus 로고
    • Alterations on the heme biosynthetic pathway from the III-V semiconductor metal, indium arsenide (InAs)
    • 9. Connor EA, Yamauchi H and Fowler BA, Alterations on the heme biosynthetic pathway from the III-V semiconductor metal, indium arsenide (InAs). Chem Biol Interact 96: 275-285, 1995.
    • (1995) Chem Biol Interact , vol.96 , pp. 275-285
    • Connor, E.A.1    Yamauchi, H.2    Fowler, B.A.3
  • 10
    • 0018612242 scopus 로고
    • Antagonistic effects of zinc and aluminum on lead inhibition of δ-aminolevulinic acid dehydratase
    • 10. Abdulla M, Svensson S and Haeger-Aronsen B, Antagonistic effects of zinc and aluminum on lead inhibition of δ-aminolevulinic acid dehydratase. Arch Environ Health 34: 464-469, 1979.
    • (1979) Arch Environ Health , vol.34 , pp. 464-469
    • Abdulla, M.1    Svensson, S.2    Haeger-Aronsen, B.3
  • 11
    • 0017357414 scopus 로고
    • Effects of aluminum, lead and zinc on δ-aminolaevulinic acid dehydratase
    • 11. Meredith PA, Moore MR and Goldberg A, Effects of aluminum, lead and zinc on δ-aminolaevulinic acid dehydratase. Enzyme 22: 22-27, 1977.
    • (1977) Enzyme , vol.22 , pp. 22-27
    • Meredith, P.A.1    Moore, M.R.2    Goldberg, A.3
  • 12
    • 0026011770 scopus 로고
    • Effects of combined exposure to aluminum and ethanol on aluminum body burden and some neuronal, hepatic and haematopoietic biochemical variables in the rat
    • 12. Flora SJS, Dhawan M and Tandon SK, Effects of combined exposure to aluminum and ethanol on aluminum body burden and some neuronal, hepatic and haematopoietic biochemical variables in the rat. Hum Exp Toxicol 10: 45-48, 1991.
    • (1991) Hum Exp Toxicol , vol.10 , pp. 45-48
    • Flora, S.J.S.1    Dhawan, M.2    Tandon, S.K.3
  • 13
    • 0027466370 scopus 로고
    • Inhibition of delta aminolevulinic acid dehydratase activity by aluminum
    • 13. Zaman K, Zaman W, Dabrowski Z and Miszta H, Inhibition of delta aminolevulinic acid dehydratase activity by aluminum. Comp Biochem Physiol 104C: 269-273, 1993.
    • (1993) Comp Biochem Physiol , vol.104 C , pp. 269-273
    • Zaman, K.1    Zaman, W.2    Dabrowski, Z.3    Miszta, H.4
  • 15
    • 0022560413 scopus 로고
    • Metabolism and possible health effects of aluminum
    • 15. Ganrot PO, Metabolism and possible health effects of aluminum. Environ Health Perspect 65: 363-441, 1986.
    • (1986) Environ Health Perspect , vol.65 , pp. 363-441
    • Ganrot, P.O.1
  • 18
    • 0011790355 scopus 로고
    • Porphyrins and related compounds
    • Ed. Tietz NW, Saunders, Philadelphia
    • 18. Labbe RF, Porphyrins and related compounds. In: Fundamentals of Clinical Chemistry (Ed. Tietz NW), pp. 455-473, Saunders, Philadelphia, 1976.
    • (1976) Fundamentals of Clinical Chemistry , pp. 455-473
    • Labbe, R.F.1
  • 19
    • 78651057641 scopus 로고
    • The occurrence and determination of δ-aminolevulic acid and porphobilinogen in urine
    • 19. Mauzerall D and Granick S, The occurrence and determination of δ-aminolevulic acid and porphobilinogen in urine. J Biol Chem 219: 435-446, 1956.
    • (1956) J Biol Chem , vol.219 , pp. 435-446
    • Mauzerall, D.1    Granick, S.2
  • 20
    • 0003518480 scopus 로고
    • Wiley-Interscience, New York
    • 20. Segel IH, Enzyme Kinetics. Wiley-Interscience, New York, 1975.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 22
    • 0022350543 scopus 로고
    • Effect of age on rat liver heme and drug metabolism
    • 22. Abraham NG, Levere RD and Freedman ML, Effect of age on rat liver heme and drug metabolism. Exp Gerontol 20: 277-281, 1985.
    • (1985) Exp Gerontol , vol.20 , pp. 277-281
    • Abraham, N.G.1    Levere, R.D.2    Freedman, M.L.3
  • 23
    • 0023819346 scopus 로고
    • Aluminum, chemical physiology and Alzheimer's disease
    • 23. Birchall JD and Chappell JS, Aluminum, chemical physiology and Alzheimer's disease. Lancet ii: 1008-1010, 1988.
    • (1988) Lancet , vol.2 , pp. 1008-1010
    • Birchall, J.D.1    Chappell, J.S.2
  • 24
    • 0022870880 scopus 로고
    • The chemistry of aluminum as related to biology and medicine
    • 24. Martin RB, The chemistry of aluminum as related to biology and medicine. Clin Chem 12: 1797-1806, 1986.
    • (1986) Clin Chem , vol.12 , pp. 1797-1806
    • Martin, R.B.1
  • 25
    • 0021338211 scopus 로고
    • Porphobilinogen synthase modification with methylmethanethiosulfonate
    • 25. Jaffe EK, Salowe SP, Chen NT and DeHaven PA, Porphobilinogen synthase modification with methylmethanethiosulfonate. J Biol Chem 259: 5032-5036, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 5032-5036
    • Jaffe, E.K.1    Salowe, S.P.2    Chen, N.T.3    DeHaven, P.A.4
  • 26
    • 0023035981 scopus 로고
    • Dissection of the early steps in the porphobilinogen synthase catalyzed reaction
    • 26. Jaffe EK and Hanes D, Dissection of the early steps in the porphobilinogen synthase catalyzed reaction. J Biol Chem 261: 9348-9353, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 9348-9353
    • Jaffe, E.K.1    Hanes, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.