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Volumn 175, Issue 6, 2005, Pages 405-411

Tyrosinase activity and hemocyanin in the hemolymph of the slipper lobster Scyllarides latus

Author keywords

Hemocyanin; Hemolimph; Purification; Scyllarides latus; Tyrosinase

Indexed keywords

HEMOCYANIN; MONOPHENOL MONOOXYGENASE;

EID: 24144445194     PISSN: 01741578     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00360-005-0002-6     Document Type: Article
Times cited : (21)

References (34)
  • 1
    • 0037229720 scopus 로고    scopus 로고
    • Hemocyte components in crustaceans convert hemocyanin into a phenoloxidase-like enzyme
    • Adachi K, Hirata T, Nishioka T, Sakaguchi M (2003) Hemocyte components in crustaceans convert hemocyanin into a phenoloxidase-like enzyme. Comp Biochem Physiol B 134:135-141
    • (2003) Comp Biochem Physiol B , vol.134 , pp. 135-141
    • Adachi, K.1    Hirata, T.2    Nishioka, T.3    Sakaguchi, M.4
  • 2
    • 0032566322 scopus 로고    scopus 로고
    • Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme
    • Banci L, Benedetto M, Bertini I, Delconte R, Piccioli M, Viezzoli MS (1998) Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme. Biochemistry 37:11780-11791
    • (1998) Biochemistry , vol.37 , pp. 11780-11791
    • Banci, L.1    Benedetto, M.2    Bertini, I.3    Delconte, R.4    Piccioli, M.5    Viezzoli, M.S.6
  • 3
    • 0036934041 scopus 로고    scopus 로고
    • Origin and evolution of arthropod hemocyanins and related proteins
    • Burmester T (2002) Origin and evolution of arthropod hemocyanins and related proteins. J Comp Physiol B 172:95-117
    • (2002) J Comp Physiol B , vol.172 , pp. 95-117
    • Burmester, T.1
  • 4
    • 1242277861 scopus 로고    scopus 로고
    • Evolutionary history and diversity of arthropod hemocyanins
    • Burmester T (2004) Evolutionary history and diversity of arthropod hemocyanins. Micron 35:121-122
    • (2004) Micron , vol.35 , pp. 121-122
    • Burmester, T.1
  • 5
    • 0028731907 scopus 로고
    • Biocatalysis with polyphenol oxidase: A review
    • Burton SG (1994) Biocatalysis with polyphenol oxidase: a review. Catal Today 22:459-487
    • (1994) Catal Today , vol.22 , pp. 459-487
    • Burton, S.G.1
  • 6
    • 0032476016 scopus 로고    scopus 로고
    • Tarantula hemocyanin shows phenoloxidase activity
    • Decker H, Rimke T (1998) Tarantula hemocyanin shows phenoloxidase activity. J Biol Chem 273:25889-25892
    • (1998) J Biol Chem , vol.273 , pp. 25889-25892
    • Decker, H.1    Rimke, T.2
  • 7
    • 0034255667 scopus 로고    scopus 로고
    • Tyrosinase/catecholoxidase activity of hemocyanins: Structural basis and molecular mechanism
    • Decker H, Tuczek F (2000) Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. Trends Biochem Sci 25:392-397
    • (2000) Trends Biochem Sci , vol.25 , pp. 392-397
    • Decker, H.1    Tuczek, F.2
  • 8
    • 0035947641 scopus 로고    scopus 로고
    • SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister
    • Decker H, Ryan M, Jaenicke E, Terwilliger N (2001) SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister. J Biol Chem 276:17796-17799
    • (2001) J Biol Chem , vol.276 , pp. 17796-17799
    • Decker, H.1    Ryan, M.2    Jaenicke, E.3    Terwilliger, N.4
  • 9
    • 0029835181 scopus 로고    scopus 로고
    • The dinuclear copper site structure of Agaricus bisporus tyrosinase in solution probed by X-ray absorption spectroscopy
    • Dellalonga S, Ascone I, Bianconi A, Bonfigli A, Castellano AC, Zarivi O, Miranda M (1996) The dinuclear copper site structure of Agaricus bisporus tyrosinase in solution probed by X-ray absorption spectroscopy. J Biol Chem 271:21025-21030
    • (1996) J Biol Chem , vol.271 , pp. 21025-21030
    • Dellalonga, S.1    Ascone, I.2    Bianconi, A.3    Bonfigli, A.4    Castellano, A.C.5    Zarivi, O.6    Miranda, M.7
  • 11
    • 0013915626 scopus 로고    scopus 로고
    • Chemical studies on hemocyanins. I. Amino acid composition
    • Ghiretti-Magaldi A, Nuzzolo C, Ghiretti F (1996) Chemical studies on hemocyanins. I. Amino acid composition. Biochemistry 5:1943-1951
    • (1996) Biochemistry , vol.5 , pp. 1943-1951
    • Ghiretti-Magaldi, A.1    Nuzzolo, C.2    Ghiretti, F.3
  • 13
    • 0032053588 scopus 로고    scopus 로고
    • Intermediate filament assembly - Fibrillogenesis is driven by decisive dimer-dimer interactions
    • Herrmann H, Aebi U (1998) Intermediate filament assembly - fibrillogenesis is driven by decisive dimer-dimer interactions. Curr Opin Struct Biol 8:177-185
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 177-185
    • Herrmann, H.1    Aebi, U.2
  • 14
    • 0033080359 scopus 로고    scopus 로고
    • Interaction of the capsid protein p24 (HIV-1) with sequence-derived peptides: Influence on p24 dimerization
    • Hilpert K, Belke J, Scholz C, Misselwitz R, Schneider-Mergener J, Hohne W (1999) Interaction of the capsid protein p24 (HIV-1) with sequence-derived peptides: influence on p24 dimerization. Virology 254:6-10
    • (1999) Virology , vol.254 , pp. 6-10
    • Hilpert, K.1    Belke, J.2    Scholz, C.3    Misselwitz, R.4    Schneider-Mergener, J.5    Hohne, W.6
  • 15
    • 0029113001 scopus 로고
    • Hemocyanins
    • Anfinsen CB, Edsall JT, Richards FM, Eisenberg DS (eds) Academic, London
    • van Holde KE, Miller KI (1995) Hemocyanins. In: Anfinsen CB, Edsall JT, Richards FM, Eisenberg DS (eds) Advances in Protein Chemistry vol 47. Academic, London, pp 1-81
    • (1995) Advances in Protein Chemistry , vol.47 , pp. 1-81
    • Van Holde, K.E.1    Miller, K.I.2
  • 16
    • 0035844294 scopus 로고    scopus 로고
    • Hemocyanins and invertebrate evolution
    • van Holde KE, Miller Kl, Decker H (2001) Hemocyanins and invertebrate evolution. J Biol Chem 276:15563-15566
    • (2001) J Biol Chem , vol.276 , pp. 15563-15566
    • Van Holde, K.E.1    Miller, Kl.2    Decker, H.3
  • 17
    • 0037965469 scopus 로고    scopus 로고
    • Tyrosinases from crustaceans form hexamers
    • Jaenicke E, Decker H (2003) Tyrosinases from crustaceans form hexamers. Biochem J 371:515-523
    • (2003) Biochem J , vol.371 , pp. 515-523
    • Jaenicke, E.1    Decker, H.2
  • 18
    • 1242300244 scopus 로고    scopus 로고
    • Conversion of crustacean hemocyanin to catecholoxidase
    • Jaenicke E, Decker H (2004) Conversion of crustacean hemocyanin to catecholoxidase. Micron 35:89-90
    • (2004) Micron , vol.35 , pp. 89-90
    • Jaenicke, E.1    Decker, H.2
  • 20
    • 0026751906 scopus 로고
    • Isolation and characterization of hemolymph phenoloxidase from Heliothis virescens larvae
    • Lockey TD, Ourth DD (1992) Isolation and characterization of hemolymph phenoloxidase from Heliothis virescens larvae. Comp Biochem Physiol B 102:891-896
    • (1992) Comp Biochem Physiol B , vol.102 , pp. 891-896
    • Lockey, T.D.1    Ourth, D.D.2
  • 21
    • 0025231704 scopus 로고
    • Sodium dodecyl sulfate activation of a plant polyphenoloxidase. Effect of sodium dodecyl sulfate on enzymatic and physical characteristics of purified broad bean polyphenoloxidase
    • Moore BM, Flurkey WH (1990) Sodium dodecyl sulfate activation of a plant polyphenoloxidase. Effect of sodium dodecyl sulfate on enzymatic and physical characteristics of purified broad bean polyphenoloxidase. J Biol Chem 265:4982-4986
    • (1990) J Biol Chem , vol.265 , pp. 4982-4986
    • Moore, B.M.1    Flurkey, W.H.2
  • 22
    • 0034703094 scopus 로고    scopus 로고
    • A link between blood coagulation and prophenol oxidase activation in arthropod host defense
    • Nagai T, Kawabata S (2000) A link between blood coagulation and prophenol oxidase activation in arthropod host defense. J Biol Chem 275:29264-29267
    • (2000) J Biol Chem , vol.275 , pp. 29264-29267
    • Nagai, T.1    Kawabata, S.2
  • 23
    • 0035920142 scopus 로고    scopus 로고
    • Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides
    • Nagai T, Osaki T, Kawabata S (2001) Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides. J Biol Chem 276:27166-27170
    • (2001) J Biol Chem , vol.276 , pp. 27166-27170
    • Nagai, T.1    Osaki, T.2    Kawabata, S.3
  • 24
    • 0029871610 scopus 로고    scopus 로고
    • On the presence of prophenoloxidase in the hemolymph of the horseshoe crab, Limulus
    • Nellaiappan K, Sugumaran M (1996) On the presence of prophenoloxidase in the hemolymph of the horseshoe crab, Limulus. Comp Biochem Physiol B 113:163-168
    • (1996) Comp Biochem Physiol B , vol.113 , pp. 163-168
    • Nellaiappan, K.1    Sugumaran, M.2
  • 25
    • 0037440365 scopus 로고    scopus 로고
    • Latent phenoloxidase activity and N-terminal amino acid sequence of hemocyanin from Bathynomus giganteus, a primitive crustacean
    • Pless DD, Aguilar MB, Falcon A, Lozano-Alvarez E, de la Cotera EPH (2003) Latent phenoloxidase activity and N-terminal amino acid sequence of hemocyanin from Bathynomus giganteus, a primitive crustacean. Arch Biochem Biophys 409:402-410
    • (2003) Arch Biochem Biophys , vol.409 , pp. 402-410
    • Pless, D.D.1    Aguilar, M.B.2    Falcon, A.3    Lozano-Alvarez, E.4    De La Cotera, E.P.H.5
  • 28
    • 0032491185 scopus 로고    scopus 로고
    • The enzymatic properties of Octopus vulgaris hemocyanin: o-diphenol oxidase activity
    • Salvato B, Santamaria M, Beltramini M, Alzuet G, Casella L (1998) The enzymatic properties of Octopus vulgaris hemocyanin: o-diphenol oxidase activity. Biochemistry 37:14065-14077
    • (1998) Biochemistry , vol.37 , pp. 14065-14077
    • Salvato, B.1    Santamaria, M.2    Beltramini, M.3    Alzuet, G.4    Casella, L.5
  • 32
    • 0035059407 scopus 로고    scopus 로고
    • Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus
    • Wang RG, Lee SY, Cerenius L, Soderhall K (2001) Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus. Eur J Biochem 268:895-902
    • (2001) Eur J Biochem , vol.268 , pp. 895-902
    • Wang, R.G.1    Lee, S.Y.2    Cerenius, L.3    Soderhall, K.4
  • 33
    • 0025910929 scopus 로고
    • New assay for the tyrosinase hydroxylase and dopa oxidase activities of tyrosinase
    • Winder AJ, Harris H (1991) New assay for the tyrosinase hydroxylase and dopa oxidase activities of tyrosinase. Eur J Biochem 198:317-321
    • (1991) Eur J Biochem , vol.198 , pp. 317-321
    • Winder, A.J.1    Harris, H.2
  • 34
    • 0029981365 scopus 로고    scopus 로고
    • The o-diphenol oxidase activity of arthropod hemocyanin
    • Zlateva T, Dimuro P, Salvato B, Beltramini M (1996) The o-diphenol oxidase activity of arthropod hemocyanin. FEBS Lett 384:251-254
    • (1996) FEBS Lett , vol.384 , pp. 251-254
    • Zlateva, T.1    Dimuro, P.2    Salvato, B.3    Beltramini, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.