메뉴 건너뛰기




Volumn 137, Issue 4, 2004, Pages 307-311

Inhibition by tributyltin of herring skeletal muscle lactate dehydrogenase activity

Author keywords

Bovine serum albumin; BSA protection; Fish; Herring; Lactate dehydrogenase; LDH A4; Skeletal muscle; TBT; Tributyltin

Indexed keywords

BOVINE SERUM ALBUMIN; LACTATE DEHYDROGENASE ISOENZYME; TRIBUTYLTIN CHLORIDE;

EID: 3042655071     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2004.02.005     Document Type: Article
Times cited : (8)

References (17)
  • 2
    • 0030039627 scopus 로고    scopus 로고
    • Ecotoxicology of organotin compounds
    • Fent K. Ecotoxicology of organotin compounds. Crit. Rev. Toxicol. 26:1996;1-117
    • (1996) Crit. Rev. Toxicol. , vol.26 , pp. 1-117
    • Fent, K.1
  • 3
    • 0037333267 scopus 로고    scopus 로고
    • Enzyme activities in fish spermatozoa with focus on lactate dehydrogenase isoenzymes from herring Clupea harengus
    • Gronczewska J., Zietara M.S., Biegniewska A., Skorkowski E.F. Enzyme activities in fish spermatozoa with focus on lactate dehydrogenase isoenzymes from herring Clupea harengus. Comp. Biochem. Physiol. B134:2003;399-406
    • (2003) Comp. Biochem. Physiol. , vol.134 , pp. 399-406
    • Gronczewska, J.1    Zietara, M.S.2    Biegniewska, A.3    Skorkowski, E.F.4
  • 4
    • 0037313798 scopus 로고    scopus 로고
    • Quantitative determination of creatine kinase release from herring (Clupea harengus) spermatozoa induced by tributyltin
    • Grzyb K., Rychlowski M., Biegniewska A., Skorkowski E.F. Quantitative determination of creatine kinase release from herring (Clupea harengus) spermatozoa induced by tributyltin. Comp. Biochem. Physiol. C134:2003;207-213
    • (2003) Comp. Biochem. Physiol. , vol.134 , pp. 207-213
    • Grzyb, K.1    Rychlowski, M.2    Biegniewska, A.3    Skorkowski, E.F.4
  • 6
    • 0016849248 scopus 로고
    • Evolution of a gene. Multiple genes for LDH isozymes provide a model of the evolution of gene structure, function and regulation
    • Markert C.L., Shaklee J.B., Whitt G.C. Evolution of a gene. Multiple genes for LDH isozymes provide a model of the evolution of gene structure, function and regulation. Science. 189:1975;102-114
    • (1975) Science , vol.189 , pp. 102-114
    • Markert, C.L.1    Shaklee, J.B.2    Whitt, G.C.3
  • 7
    • 0041833393 scopus 로고    scopus 로고
    • Early life exposure to environmental levels of the aromatase inhibitor tributyltin causes masculinisation and irreversible sperm damage in zebrafish (Danio rerio)
    • McAllister B.G., Kime D.E. Early life exposure to environmental levels of the aromatase inhibitor tributyltin causes masculinisation and irreversible sperm damage in zebrafish (Danio rerio). Aquat. Toxicol. 65:2003;309-316
    • (2003) Aquat. Toxicol. , vol.65 , pp. 309-316
    • McAllister, B.G.1    Kime, D.E.2
  • 8
    • 0036131154 scopus 로고    scopus 로고
    • Effect of tributyltin on adenylate content and enzyme activities of teleost sperm: A biochemical approach to study the mechanisms of toxicant reduced spermatozoa motility
    • Rurangwa E., Biegniewska A., Slomińska E., Skorkowski E.F., Ollevier F. Effect of tributyltin on adenylate content and enzyme activities of teleost sperm: a biochemical approach to study the mechanisms of toxicant reduced spermatozoa motility. Comp. Biochem. Physiol. C131:2002;335-344
    • (2002) Comp. Biochem. Physiol. , vol.131 , pp. 335-344
    • Rurangwa, E.1    Biegniewska, A.2    Slomińska, E.3    Skorkowski, E.F.4    Ollevier, F.5
  • 11
    • 0022655806 scopus 로고
    • Organotin-protein interactions
    • Siebenlist K.R., Taketa F. Organotin-protein interactions. Biochem. J. 233:1986;471-477
    • (1986) Biochem. J. , vol.233 , pp. 471-477
    • Siebenlist, K.R.1    Taketa, F.2
  • 12
    • 0018121934 scopus 로고
    • Refinement of the Coomassie Blue method of protein quantitation
    • Spector T. Refinement of the Coomassie Blue method of protein quantitation. Analyt. Biochem. 86:1978;142-146
    • (1978) Analyt. Biochem. , vol.86 , pp. 142-146
    • Spector, T.1
  • 13
    • 0032537608 scopus 로고    scopus 로고
    • Cytochrome c release and caspase activation in hydrogen peroxide- and tributyltin-induced apoptosis
    • Stridh H., Kimland M., Jones D.P., Orrenius S., Hampton M.B. Cytochrome c release and caspase activation in hydrogen peroxide- and tributyltin-induced apoptosis. FEBS Lett. 429:1998;351-355
    • (1998) FEBS Lett. , vol.429 , pp. 351-355
    • Stridh, H.1    Kimland, M.2    Jones, D.P.3    Orrenius, S.4    Hampton, M.B.5
  • 14
    • 0033590122 scopus 로고    scopus 로고
    • The role of calcium in pre- and postmitochondrial events in tributyltin-induced T-cell apoptosis
    • Stridh H., Gigliotti D., Orrenius S., Cotgreave I. The role of calcium in pre- and postmitochondrial events in tributyltin-induced T-cell apoptosis. Biochem. Biophys. Res. Commun. 266:1999;460-465
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 460-465
    • Stridh, H.1    Gigliotti, D.2    Orrenius, S.3    Cotgreave, I.4
  • 17
    • 0028827581 scopus 로고
    • 4 isoenzyme: Effect of heat shock protein DnaK on the enzyme activity
    • 4 isoenzyme: effect of heat shock protein DnaK on the enzyme activity. Int. J. Biochem. Cell Biol. 27:1995;1169-1174
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 1169-1174
    • Zietara, M.S.1    Skorkowski, E.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.