메뉴 건너뛰기




Volumn 35, Issue 3, 2003, Pages 219-224

Purification, characterization and biological activity of an L-amino acid oxidase from Trimeresurus mucrosquamatus venom

Author keywords

Antibacterial activity; Cytotoxicity; L amino acid oxidase; Platelet aggregation; Trimeresurus mucrosquamatus

Indexed keywords

AMINO ACID OXIDASE; CATALASE; HYDROGEN PEROXIDE; SCAVENGER; SEPHADEX; SNAKE VENOM; VIPER VENOM;

EID: 0038559552     PISSN: 05829879     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (34)

References (32)
  • 3
    • 0023781038 scopus 로고
    • Purification and characterization of L-amino acid oxidase from the venom of Trimeresurus mucrosquamatus (Taiwan habu snake)
    • Ueda M, Chang CC, Ohno M. Purification and characterization of L-amino acid oxidase from the venom of Trimeresurus mucrosquamatus (Taiwan habu snake). Toxicon, 1988, 26: 695-706
    • (1988) Toxicon , vol.26 , pp. 695-706
    • Ueda, M.1    Chang, C.C.2    Ohno, M.3
  • 4
    • 0031710064 scopus 로고    scopus 로고
    • Characterization of an apoptosis-inducing factor in Habu snake venom as a glycyrrhizin (GL)-binding protein potently inhibited by GL in vitro
    • Abe Y, Shimoyama Y, Munakata H, Ito J, Nagata N, Ohtsuki K. Characterization of an apoptosis-inducing factor in Habu snake venom as a glycyrrhizin (GL)-binding protein potently inhibited by GL in vitro. Biol Pharm Bull, 1998, 21: 924-927
    • (1998) Biol Pharm Bull , vol.21 , pp. 924-927
    • Abe, Y.1    Shimoyama, Y.2    Munakata, H.3    Ito, J.4    Nagata, N.5    Ohtsuki, K.6
  • 5
    • 0027989688 scopus 로고
    • Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasmu rhodostoma) venom
    • Ponnudurai G, Chung MC, Tan NH. Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasmu rhodostoma) venom. Arch Biochem Biophys, 1994, 313: 373-378
    • (1994) Arch Biochem Biophys , vol.313 , pp. 373-378
    • Ponnudurai, G.1    Chung, M.C.2    Tan, N.H.3
  • 6
    • 0034823588 scopus 로고    scopus 로고
    • L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma. Comparative sequence analysis and characterization of active and inactive forms of the enzyme
    • MacHeroux P, Seth O, Bollschweiler C, Schwarz M, Kurfurst M, Au LC, Ghisla S. L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma. Comparative sequence analysis and characterization of active and inactive forms of the enzyme. Eur J Biochem, 2001, 268 (6): 1679-1686
    • (2001) Eur J Biochem , vol.268 , Issue.6 , pp. 1679-1686
    • MacHeroux, P.1    Seth, O.2    Bollschweiler, C.3    Schwarz, M.4    Kurfurst, M.5    Au, L.C.6    Ghisla, S.7
  • 7
    • 0030792457 scopus 로고    scopus 로고
    • Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)
    • Ahn MY, Lee BM, Kim YS. Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah). Int J Biochem Cell Biol, 1997, 29: 911-919
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 911-919
    • Ahn, M.Y.1    Lee, B.M.2    Kim, Y.S.3
  • 8
    • 0033567358 scopus 로고    scopus 로고
    • Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix loticinctus snake venom: Preliminary crystallographic data
    • Souza DH, Eugenio LM, Fletcher JE, Jiang MS, Garratt RC, Oliva G, Selistre-de-Araujo HS. Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix loticinctus snake venom: Preliminary crystallographic data. Arch Biochem Biophys, 1999, 368: 285-290
    • (1999) Arch Biochem Biophys , vol.368 , pp. 285-290
    • Souza, D.H.1    Eugenio, L.M.2    Fletcher, J.E.3    Jiang, M.S.4    Garratt, R.C.5    Oliva, G.6    Selistre-de-Araujo, H.S.7
  • 9
    • 0036396892 scopus 로고    scopus 로고
    • Purification and characterization of L-amino acid oxidase from Agkistrodon halys Pallas venom
    • Liu JW, Chai MQ, Du XY, Song JG, Zhou YC. Purification and characterization of L-amino acid oxidase from Agkistrodon halys Pallas venom. Acta Biochim Biophys Sin, 2002, 34: 305-310
    • (2002) Acta Biochim Biophys Sin , vol.34 , pp. 305-310
    • Liu, J.W.1    Chai, M.Q.2    Du, X.Y.3    Song, J.G.4    Zhou, Y.C.5
  • 10
    • 0030570468 scopus 로고    scopus 로고
    • Identification of the snake venom substance that induces apoptosis
    • Suhr SM, Kim DS. Identification of the snake venom substance that induces apoptosis. Biochem Biophys Res Commun, 1996, 224: 134-139
    • (1996) Biochem Biophys Res Commun , vol.224 , pp. 134-139
    • Suhr, S.M.1    Kim, D.S.2
  • 11
    • 0030910602 scopus 로고    scopus 로고
    • Apoxin I, a novel apoptosis-inducing factor with L-amino acid oxidase activity purified from the western diamondback rattlesnake venom
    • Torii S, Naito M, Tsuruo T. Apoxin I, a novel apoptosis-inducing factor with L-amino acid oxidase activity purified from the western diamondback rattlesnake venom. J Biol Chem, 1997, 272: 9539-9542
    • (1997) J Biol Chem , vol.272 , pp. 9539-9542
    • Torii, S.1    Naito, M.2    Tsuruo, T.3
  • 12
    • 0028045984 scopus 로고
    • Purification and characterization of L-amino acid oxidase from king cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation
    • Li ZY, Yu TF, Lian EC. Purification and characterization of L-amino acid oxidase from king cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation. Toxicon. 1994, 32: 1349-1358
    • (1994) Toxicon , vol.32 , pp. 1349-1358
    • Li, Z.Y.1    Yu, T.F.2    Lian, E.C.3
  • 13
    • 0035847123 scopus 로고    scopus 로고
    • Molecular characterization of L-amino acid oxidase from Agistrodon halys blomhoffii with special reference to platelet aggregation
    • Takatsuka H, Sakurai Y, Yoshioka A, Kokubo T, Usami Y, Suzuki M, Matsui T et al. Molecular characterization of L-amino acid oxidase from Agistrodon halys blomhoffii with special reference to platelet aggregation. Biochim Biophys Acta, 2001, 1554: 267-277
    • (2001) Biochim Biophys Acta , vol.1554 , pp. 267-277
    • Takatsuka, H.1    Sakurai, Y.2    Yoshioka, A.3    Kokubo, T.4    Usami, Y.5    Suzuki, M.6    Matsui, T.7
  • 14
    • 0034792723 scopus 로고    scopus 로고
    • Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom
    • Sakurai Y, Takasuka H, Yoshioka A, Matsui T, Suzuki M, Titanti K, Fujimura Y. Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom. Toxicon, 2001, 39: 1827-1833
    • (2001) Toxicon , vol.39 , pp. 1827-1833
    • Sakurai, Y.1    Takasuka, H.2    Yoshioka, A.3    Matsui, T.4    Suzuki, M.5    Titanti, K.6    Fujimura, Y.7
  • 15
    • 0025784241 scopus 로고
    • Antibacterial effects of different snake venoms: Purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom
    • Stiles BG, Sexton FW, Weinstein SA. Antibacterial effects of different snake venoms: Purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom. Toxicon, 1991, 29: 1129-1141
    • (1991) Toxicon , vol.29 , pp. 1129-1141
    • Stiles, B.G.1    Sexton, F.W.2    Weinstein, S.A.3
  • 16
    • 0006676698 scopus 로고
    • The edema inducing activity of Ophiophagus hannah (king cobra) venom L-amino acid oxidase
    • Tan NH, Choy SK. The edema inducing activity of Ophiophagus hannah (king cobra) venom L-amino acid oxidase. Toxicon. 1994. 32: 539
    • (1994) Toxicon , vol.32 , pp. 539
    • Tan, N.H.1    Choy, S.K.2
  • 17
    • 0034671997 scopus 로고    scopus 로고
    • Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom
    • Ali SA, Stoeva S, Abbasi A, Alam JM, Kayed R, Faigle M, Neumeister B et al. Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom. Arch Biochem Biophys, 2000, 384: 216-226
    • (2000) Arch Biochem Biophys , vol.384 , pp. 216-226
    • Ali, S.A.1    Stoeva, S.2    Abbasi, A.3    Alam, J.M.4    Kayed, R.5    Faigle, M.6    Neumeister, B.7
  • 18
    • 77957008188 scopus 로고
    • Assay of amino acid oxidase
    • Tabor H, Tabor CW eds., New York: Academic Press
    • Wellner D, Lichtenberg LA. Assay of amino acid oxidase. In: Tabor H, Tabor CW eds. Methods in Enzymology (Vol. 17B), New York: Academic Press, 1971, 593-596
    • (1971) Methods in Enzymology , vol.17 B , pp. 593-596
    • Wellner, D.1    Lichtenberg, L.A.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 1970, 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0013801195 scopus 로고
    • The gel-filtration behaviors of proteins related to their molecular weights over a wide range
    • Andrews P. The gel-filtration behaviors of proteins related to their molecular weights over a wide range. Biochem J. 1965, 96: 595-606
    • (1965) Biochem J , vol.96 , pp. 595-606
    • Andrews, P.1
  • 21
    • 78651139188 scopus 로고
    • The aggregation of blood platelets
    • Born GVR, Cross MJ. The aggregation of blood platelets. J Physiol Lond, 1963, 168: 178-195
    • (1963) J Physiol Lond , vol.168 , pp. 178-195
    • Born, G.V.R.1    Cross, M.J.2
  • 22
    • 0013902668 scopus 로고
    • Antibiotic susceptibility testing by a standardized single disk method
    • Bauer AW, Kirby WM, Sherris JC, Turck M. Antibiotic susceptibility testing by a standardized single disk method. Am J Clin Pathol, 1966, 45: 493-496
    • (1966) Am J Clin Pathol , vol.45 , pp. 493-496
    • Bauer, A.W.1    Kirby, W.M.2    Sherris, J.C.3    Turck, M.4
  • 23
    • 0023186213 scopus 로고
    • Characterization of three edema-inducing phospholipase A2 enzymes from habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristalochic acid
    • Vishwanath BS, Kini RM, Gowda TV. Characterization of three edema-inducing phospholipase A2 enzymes from habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristalochic acid. Toxicon, 1987, 25: 501-515
    • (1987) Toxicon , vol.25 , pp. 501-515
    • Vishwanath, B.S.1    Kini, R.M.2    Gowda, T.V.3
  • 24
    • 0023792919 scopus 로고
    • Evaluation of a soluble tetrazolium formazan assay for cell growth and drug sensitivity in culture using human and other tumor cell lines
    • Scudiero DA, Shoemaker RH, Paull KD, Monks A, Tierney S, Nofziger TH, Currens MJ et al. Evaluation of a soluble tetrazolium formazan assay for cell growth and drug sensitivity in culture using human and other tumor cell lines. Cancer Res, 1988, 48: 4827-4833
    • (1988) Cancer Res , vol.48 , pp. 4827-4833
    • Scudiero, D.A.1    Shoemaker, R.H.2    Paull, K.D.3    Monks, A.4    Tierney, S.5    Nofziger, T.H.6    Currens, M.J.7
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem, 1976, 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0025931518 scopus 로고
    • Snake venom variability: Methods of study, results and interpretation
    • Chippaux J P, Williams V, White J. Snake venom variability: Methods of study, results and interpretation. Toxicon. 1991, 29: 1279-1303
    • (1991) Toxicon , vol.29 , pp. 1279-1303
    • Chippaux, J.P.1    Williams, V.2    White, J.3
  • 28
    • 0030030033 scopus 로고    scopus 로고
    • Diet and snake venom evolution
    • Daltry JC, Wüster W, Thorpe RS. Diet and snake venom evolution. Nature, 1996, 379: 537-540
    • (1996) Nature , vol.379 , pp. 537-540
    • Daltry, J.C.1    Wüster, W.2    Thorpe, R.S.3
  • 29
    • 0034663814 scopus 로고    scopus 로고
    • The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
    • Pawelek PD, Cheah J, Coulombe R, Macheroux P, Ghisla S, Vrielink A. The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. EMBO J, 2000, 19: 4204-4215
    • (2000) EMBO J , vol.19 , pp. 4204-4215
    • Pawelek, P.D.1    Cheah, J.2    Coulombe, R.3    Macheroux, P.4    Ghisla, S.5    Vrielink, A.6
  • 32
    • 0033033686 scopus 로고    scopus 로고
    • Comparison of the apoptotic pathways induced by L-amino acid oxidase and hydrogen peroxide
    • Suhr SM, Kim DS. Comparison of the apoptotic pathways induced by L-amino acid oxidase and hydrogen peroxide. J Biochem, 1999, 125: 305-309
    • (1999) J Biochem , vol.125 , pp. 305-309
    • Suhr, S.M.1    Kim, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.