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Volumn 46, Issue 8, 2005, Pages 907-917

Purification, primary structures and evolution of coagulant proteases from Deinagkistrodon actus venom

Author keywords

cDNA cloning; Deinagkistrodon actus; Evolution; Phylogeny; Primary structure; Purification; Venom coagulant protease

Indexed keywords

3,4 DICHLOROISOCOUMARIN; ACTIBIN; AMIDASE; AMINO ACID; ANILIDE; COAGULATING AGENT; COMPLEMENTARY DNA; FIBRINOGEN; GLYCOPROTEIN; NUCLEOTIDE; PROTEINASE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SNAKE VENOM; THROMBIN; TOSYLARGININE METHYL ESTER; UNCLASSIFIED DRUG;

EID: 28444461776     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2005.08.016     Document Type: Article
Times cited : (7)

References (51)
  • 1
    • 0027201808 scopus 로고
    • Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from venom of Callaselasma rhodostoma
    • L.C. Au, S.-B. Lin, J.-S. Chou, G.-W. The, K.-J. Chang, and C.-M. Shin Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from venom of Callaselasma rhodostoma Biochem. J. 294 1993 387 390
    • (1993) Biochem. J. , vol.294 , pp. 387-390
    • Au, L.C.1    Lin, S.-B.2    Chou, J.-S.3    The, G.-W.4    Chang, K.-J.5    Shin, C.-M.6
  • 2
    • 0028673152 scopus 로고
    • Classification of peptidases
    • A.J. Barrett Academic Press New York
    • A.J. Barrett Classification of peptidases A.J. Barrett Methods in Enzymology vol. 244 1994 Academic Press New York 1 15
    • (1994) Methods in Enzymology , vol.244 , pp. 1-15
    • Barrett, A.J.1
  • 3
    • 0021710691 scopus 로고
    • Rapid analysis of amino acids using pre-column derivatization
    • B.A. Bidlingmeyer, S.A. Cohen, and T.L. Tarvin Rapid analysis of amino acids using pre-column derivatization J. Chromatogr. 336 1984 93 104
    • (1984) J. Chromatogr. , vol.336 , pp. 93-104
    • Bidlingmeyer, B.A.1    Cohen, S.A.2    Tarvin, T.L.3
  • 4
    • 0002987063 scopus 로고
    • X-Ray crystal structure of human α-thrombin and of the human thrombin-hirudin complex
    • L.J. Berliner Plenum Press New York
    • W. Bode, R. Huber, T.J. Rydel, and A. Tulinskj X-Ray crystal structure of human α-thrombin and of the human thrombin-hirudin complex L.J. Berliner Thrombin: Structure and Function 1992 Plenum Press New York 3 62
    • (1992) Thrombin: Structure and Function , pp. 3-62
    • Bode, W.1    Huber, R.2    Rydel, T.J.3    Tulinskj, A.4
  • 5
    • 0026503083 scopus 로고
    • Amino acid sequence determination of ancrod, the thrombin-like α-fibrinogenase from venom of Agkistrodon rhodostoma
    • W. Burkhart, G.F.H. Smith, J.-L. Su, I. Parikh, and H. Le Vine III Amino acid sequence determination of ancrod, the thrombin-like α-fibrinogenase from venom of Agkistrodon rhodostoma FEBS Lett. 297 1992 297 301
    • (1992) FEBS Lett. , vol.297 , pp. 297-301
    • Burkhart, W.1    Smith, G.F.H.2    Su, J.-L.3    Parikh, I.4    Le Vine III, H.5
  • 6
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched by ribonuclease
    • J.M. Chirgwin, A.E. Przybyla, R.J. MacDonald, and W.J. Rutter Isolation of biologically active ribonucleic acid from sources enriched by ribonuclease Biochemistry 18 1979 5294 5299
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 9
    • 28444482914 scopus 로고
    • Fibrinogen and fibrin
    • L. Lorand Academic Press New York
    • R.F. Doolittle Fibrinogen and fibrin L. Lorand Methods in Enzymology vol. 45B 1976 Academic Press New York 205 213
    • (1976) Methods in Enzymology , vol.45 , pp. 205-213
    • Doolittle, R.F.1
  • 10
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • B.F. Erlanger, N. Kokowsky, and W. Cohen The preparation and properties of two new chromogenic substrates of trypsin Arch. Biochem. Biophys. 95 1961 271 278
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 12
    • 0015497788 scopus 로고
    • Observations concerning the substrate specificity of arvin
    • T. Exner, and J.L. Koppel Observations concerning the substrate specificity of arvin Biochim. Biophys. Acta 258 1972 825 829
    • (1972) Biochim. Biophys. Acta , vol.258 , pp. 825-829
    • Exner, T.1    Koppel, J.L.2
  • 13
    • 0015611481 scopus 로고
    • Studies on the coagulant enzyme from Agkistrodon rhodostoma venom
    • M.W.C. Hatton Studies on the coagulant enzyme from Agkistrodon rhodostoma venom Biochem. J. 131 1973 799 807
    • (1973) Biochem. J. , vol.131 , pp. 799-807
    • Hatton, M.W.C.1
  • 14
    • 0023195836 scopus 로고
    • Use of N-glycanase to release asparagine-linked oligosaccharides for structural analysis
    • S. Hirani, R.J. Bernasconi, and J.R. Rasmussen Use of N-glycanase to release asparagine-linked oligosaccharides for structural analysis Anal. Biochem. 485 1987 492
    • (1987) Anal. Biochem. , vol.485 , pp. 492
    • Hirani, S.1    Bernasconi, R.J.2    Rasmussen, J.R.3
  • 15
    • 0023644641 scopus 로고
    • Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin like snake venom enzyme
    • N. Itoh, N. Tanaka, S. Mihashi, and I. Yamashina Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin like snake venom enzyme J. Biol. Chem. 262 1987 3132 3135
    • (1987) J. Biol. Chem. , vol.262 , pp. 3132-3135
    • Itoh, N.1    Tanaka, N.2    Mihashi, S.3    Yamashina, I.4
  • 16
    • 0014553632 scopus 로고
    • The rate of molecular evolution considered from the standpoint of population genetics
    • M. Kimura The rate of molecular evolution considered from the standpoint of population genetics Proc. Natl Acad. Sci. USA 63 1969 1181 1188
    • (1969) Proc. Natl Acad. Sci. USA , vol.63 , pp. 1181-1188
    • Kimura, M.1
  • 18
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • S. Kumar, K. Tamura, I.B. Jakobsen, and M. Nei MEGA2: molecular evolutionary genetics analysis software Bioinformatics 17 2001 1244 1245
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0027305178 scopus 로고
    • The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachasis muta muta)
    • A. Magalhaes, B.C.B.D.F. Fonseca, C.R. Diniz, J. Gilroy, and M. Richardson The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachasis muta muta) FEBS Lett. 329 1993 116 120
    • (1993) FEBS Lett. , vol.329 , pp. 116-120
    • Magalhaes, A.1    Fonseca, B.C.B.D.F.2    Diniz, C.R.3    Gilroy, J.4    Richardson, M.5
  • 23
    • 0001756741 scopus 로고
    • Complete primary structure of prothrombin: Isolation, structure and reactivity of ten carboxylated glutamic acid residues and regulation of prothrombin activation by thrombin
    • E. Reich D.B. Rifkin E. Shaw Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • S. Magnusson, T.W. Peterson, L. Sottrup-Jensen, and H. Claeys Complete primary structure of prothrombin: isolation, structure and reactivity of ten carboxylated glutamic acid residues and regulation of prothrombin activation by thrombin E. Reich D.B. Rifkin E. Shaw Proteases and Biological Control 1975 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 123 149
    • (1975) Proteases and Biological Control , pp. 123-149
    • Magnusson, S.1    Peterson, T.W.2    Sottrup-Jensen, L.3    Claeys, H.4
  • 24
    • 0002805558 scopus 로고
    • Molecular Cloning
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • T. Maniatis, E.F. Fritsch, and J. Sambrook Molecular Cloning A Laboratory Manual 1989 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • (1989) A Laboratory Manual
    • Maniatis, T.1    Fritsch, E.F.2    Sambrook, J.3
  • 25
    • 0007663470 scopus 로고
    • Nucleotide sequence divergence and functional constraint in mRNA evolution
    • T. Miyata, Y. Teruo, and T. Nishida Nucleotide sequence divergence and functional constraint in mRNA evolution Proc. Natl Acad. Sci. USA 77 1980 7328 7332
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 7328-7332
    • Miyata, T.1    Teruo, Y.2    Nishida, T.3
  • 26
    • 0024086803 scopus 로고
    • Graphic presentation of amino acid composition with a modified radar chart
    • K. Nakamura, and T. Furukohri Graphic presentation of amino acid composition with a modified radar chart J. Jpn. Biochem. Soc. (Seikagaku) 60 1988 1060 1063
    • (1988) J. Jpn. Biochem. Soc. (Seikagaku) , vol.60 , pp. 1060-1063
    • Nakamura, K.1    Furukohri, T.2
  • 29
    • 0022507362 scopus 로고
    • Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions
    • M. Nei, and T. Gojobori Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions Mol. Biol. Evol. 3 1986 418 426
    • (1986) Mol. Biol. Evol. , vol.3 , pp. 418-426
    • Nei, M.1    Gojobori, T.2
  • 30
    • 0028947353 scopus 로고
    • Primary structure of a coagulant enzyme, bilionebin, from Agkistrodon bilineatus venom
    • T. Nikai, A. Ohara, Y. Komori, J.W. Fox, and H. Sugihara Primary structure of a coagulant enzyme, bilionebin, from Agkistrodon bilineatus venom Arch. Biochem. Biophys. 318 1995 89 96
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 89-96
    • Nikai, T.1    Ohara, A.2    Komori, Y.3    Fox, J.W.4    Sugihara, H.5
  • 32
    • 0020132173 scopus 로고
    • Correlation of the amino acid composition of a protein to its structural and biological characters
    • K. Nishikawa, and T. Ooi Correlation of the amino acid composition of a protein to its structural and biological characters J. Biochem. (Tokyo) 91 1982 1821 1824
    • (1982) J. Biochem. (Tokyo) , vol.91 , pp. 1821-1824
    • Nishikawa, K.1    Ooi, T.2
  • 34
    • 0017243179 scopus 로고
    • Ancrod, the coagulating enzyme from Malayan Pit viper (Agkistrodon rhodostoma) venom
    • L. Lorand Academic Press New York
    • C. Nolan, L.S. Hall, and G.H. Barlow Ancrod, the coagulating enzyme from Malayan Pit viper (Agkistrodon rhodostoma) venom L. Lorand Methods in Enzymology vol. 45B 1976 Academic Press New York 205 213
    • (1976) Methods in Enzymology , vol.45 , pp. 205-213
    • Nolan, C.1    Hall, L.S.2    Barlow, G.H.3
  • 35
    • 0028593547 scopus 로고
    • Purification and characterization of a coagulant enzyme, okinaxobin II, from Trimeresurus okinavensis (himehabu snake) venom which releases fibrinopeptides a and B
    • T. Nose, Y. Shimohigashi, S. Hattori, H. Kihara, and M. Ohno Purification and characterization of a coagulant enzyme, okinaxobin II, from Trimeresurus okinavensis (himehabu snake) venom which releases fibrinopeptides A and B Toxicon 34 1994 1509 1520
    • (1994) Toxicon , vol.34 , pp. 1509-1520
    • Nose, T.1    Shimohigashi, Y.2    Hattori, S.3    Kihara, H.4    Ohno, M.5
  • 36
    • 0001643609 scopus 로고
    • The effect of Formosan snake venom on blood coagulation in vitro
    • C. Ouyang The effect of Formosan snake venom on blood coagulation in vitro Formosan Med. Assoc. 56 1957 435 447
    • (1957) Formosan Med. Assoc. , vol.56 , pp. 435-447
    • Ouyang, C.1
  • 37
    • 0015247220 scopus 로고
    • Purification and properties of the thrombin like principle of Agkistridon acutus venom and its comparison with bovine thrombin
    • C. Ouyang, J.-S. Hong, and C.-M. Teng Purification and properties of the thrombin like principle of Agkistridon acutus venom and its comparison with bovine thrombin Thromb. Diath. Haemorrh. 26 1971 224 234
    • (1971) Thromb. Diath. Haemorrh. , vol.26 , pp. 224-234
    • Ouyang, C.1    Hong, J.-S.2    Teng, C.-M.3
  • 38
    • 0018396593 scopus 로고
    • The clotting activity of the thrombin-like enzyme of Agkistrodon acutus (Hundred pace snake) venom
    • C. Ouyang, Y.-C. Chen, and C.-M. Teng The clotting activity of the thrombin-like enzyme of Agkistrodon acutus (Hundred pace snake) venom Toxicon 17 1979 313 316
    • (1979) Toxicon , vol.17 , pp. 313-316
    • Ouyang, C.1    Chen, Y.-C.2    Teng, C.-M.3
  • 39
    • 0035998326 scopus 로고    scopus 로고
    • Amino acid sequence of a thrombin like enzyme, elegaxobin, from the venom of Trimeresurus elegans (Sakishima-habu)
    • E. Oyama, and H. Takahashi Amino acid sequence of a thrombin like enzyme, elegaxobin, from the venom of Trimeresurus elegans (Sakishima-habu) Toxicon 40 2002 959 970
    • (2002) Toxicon , vol.40 , pp. 959-970
    • Oyama, E.1    Takahashi, H.2
  • 41
    • 0025859351 scopus 로고
    • Thrombin-like enzymes from snake venom: An inventory
    • H. Pirkle, and K. Stocker Thrombin-like enzymes from snake venom: an inventory Thromb. Haemost. 65 1991 444 450
    • (1991) Thromb. Haemost. , vol.65 , pp. 444-450
    • Pirkle, H.1    Stocker, K.2
  • 42
    • 0032972599 scopus 로고    scopus 로고
    • DnaSP version 3: An integrated program for molecular population genetics and molecular evolution analysis
    • J. Rozas, and R. Rozas DnaSP version 3: an integrated program for molecular population genetics and molecular evolution analysis Bioinformatics 15 1999 174 175
    • (1999) Bioinformatics , vol.15 , pp. 174-175
    • Rozas, J.1    Rozas, R.2
  • 43
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for the reconstructing phylogenetic tree
    • N. Saitou, and M. Nei The neighbor-joining method: a new method for the reconstructing phylogenetic tree Mol. Biol. Evol. 4 1987 406 425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 44
    • 0022384286 scopus 로고
    • Purification and characterization of a coagulant enzyme from Trimeresurus flavoviridis venom
    • T.-C. Shieh, S. Kawabata, H. Kihara, M. Ohno, and S. Iwanaga Purification and characterization of a coagulant enzyme from Trimeresurus flavoviridis venom J. Biochem. (Tokyo) 98 1985 713 721
    • (1985) J. Biochem. (Tokyo) , vol.98 , pp. 713-721
    • Shieh, T.-C.1    Kawabata, S.2    Kihara, H.3    Ohno, M.4    Iwanaga, S.5
  • 45
    • 0023883275 scopus 로고
    • Amino acid sequence of a coagulant enzyme, flavoxobin, from Trimeresurus flavoviridis venom
    • T.-C. Shieh, S. Kawabata, H. Kihara, M. Ohno, and S. Iwanaga Amino acid sequence of a coagulant enzyme, flavoxobin, from Trimeresurus flavoviridis venom J. Biochem. (Tokyo) 103 1988 596 605
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 596-605
    • Shieh, T.-C.1    Kawabata, S.2    Kihara, H.3    Ohno, M.4    Iwanaga, S.5
  • 46
    • 28444437182 scopus 로고
    • Purification and characterization of α-specific thrombin-like enzymes from the venoms of middle asian pit viper snakes Agkistrodon halis halis and Agkistrodon halis blomhoffii
    • D.A. Solovyov, and T.P. Ugarova Purification and characterization of α-specific thrombin-like enzymes from the venoms of middle asian pit viper snakes Agkistrodon halis halis and Agkistrodon halis blomhoffii Biochemistry (Moscow) 58 1993 1221 1233
    • (1993) Biochemistry (Moscow) , vol.58 , pp. 1221-1233
    • Solovyov, D.A.1    Ugarova, T.P.2
  • 47
    • 0015871755 scopus 로고
    • Glycoproteins
    • Aufinsen, G.B., Edsal, J.T., Richards, F.M. (Eds.), Academic Press, New York
    • Spiro, R.G., 1973. Glycoproteins. In: Aufinsen, G.B., Edsal, J.T., Richards, F.M. (Eds.), Advances in Protein Chemistry, vol. 27, Academic Press, New York, pp. 349-407
    • (1973) Advances in Protein Chemistry , vol.27 , pp. 349-407
    • Spiro, R.G.1
  • 49
    • 0035865501 scopus 로고    scopus 로고
    • Serine protease isoforms of Deinagkistrodon acutus venom; Cloning, sequencing and phylogenetic analysis
    • Y.-M. Wang, S.-R. Wang, and I.-H. Tsai Serine protease isoforms of Deinagkistrodon acutus venom; cloning, sequencing and phylogenetic analysis Biochem. J. 354 2001 161 168
    • (2001) Biochem. J. , vol.354 , pp. 161-168
    • Wang, Y.-M.1    Wang, S.-R.2    Tsai, I.-H.3
  • 50
    • 0035175008 scopus 로고    scopus 로고
    • Trimeresurus flavoviridis (habu snake) venom induces human erythrocytes lysis through lipolysis, complement activation and decreased membrane expression of CD55 and CD59
    • C. Yamamoto, D. Tsuru, N. Oda-Ueda, M. Ohno, S. Hattori, and S.-T. Kim Trimeresurus flavoviridis (habu snake) venom induces human erythrocytes lysis through lipolysis, complement activation and decreased membrane expression of CD55 and CD59 Pharmacol. Toxicol. 89 2001 188 194
    • (2001) Pharmacol. Toxicol. , vol.89 , pp. 188-194
    • Yamamoto, C.1    Tsuru, D.2    Oda-Ueda, N.3    Ohno, M.4    Hattori, S.5    Kim, S.-T.6
  • 51
    • 0036379701 scopus 로고    scopus 로고
    • Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase
    • C. Yamamoto, D. Tsuru, N. Oda-Ueda, M. Ohno, S. Hattori, and S.-T. Kim Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase Immunology 107 2002 111 117
    • (2002) Immunology , vol.107 , pp. 111-117
    • Yamamoto, C.1    Tsuru, D.2    Oda-Ueda, N.3    Ohno, M.4    Hattori, S.5    Kim, S.-T.6


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