메뉴 건너뛰기




Volumn 1747, Issue 2, 2005, Pages 213-220

Taiwan cobra chymotrypsin inhibitor: Cloning, functional expression and gene organization

Author keywords

Chymotrypsin inhibitor; Exon intron organization; Mutagenesis of N terminus; Naja atra

Indexed keywords

BETA BUNGAROTOXIN; CHYMOTRYPSIN INHIBITOR; COBROTOXIN; COMPLEMENTARY DNA; GENOMIC DNA; PROTEINASE INHIBITOR;

EID: 13444263657     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.11.006     Document Type: Article
Times cited : (36)

References (36)
  • 1
    • 0017196279 scopus 로고
    • Snake venom proteinase inhibitors: III. Isolation of five polypeptide inhibitors from the venoms of Hemachatus haemachatus (Ringhal's cobra) and Naja nivea (Cape cobra) and the complete amino acid sequences of two of them
    • Y. Hokama, S. Iwanaga, T. Tatsuki, and T. Suzuki Snake venom proteinase inhibitors: III. Isolation of five polypeptide inhibitors from the venoms of Hemachatus haemachatus (Ringhal's cobra) and Naja nivea (Cape cobra) and the complete amino acid sequences of two of them J. Biochem. 79 1976 559 578
    • (1976) J. Biochem. , vol.79 , pp. 559-578
    • Hokama, Y.1    Iwanaga, S.2    Tatsuki, T.3    Suzuki, T.4
  • 2
    • 0016282795 scopus 로고
    • Snake venom proteinase inhibitors: II. Chemical structure of inhibitor II isolated from the venom of Russell's viper (Viper russelli)
    • H. Takahashi, S. Iwanaga, T. Kitagawa, Y. Hokama, and T. Suzuki Snake venom proteinase inhibitors: II. Chemical structure of inhibitor II isolated from the venom of Russell's viper (Viper russelli) J. Biochem. 76 1974 721 733
    • (1974) J. Biochem. , vol.76 , pp. 721-733
    • Takahashi, H.1    Iwanaga, S.2    Kitagawa, T.3    Hokama, Y.4    Suzuki, T.5
  • 3
    • 0020955346 scopus 로고
    • Serine proteinase inhibitors from Viper ammodytes venom. Isolation and kinetic studies
    • A. Ritonja, V. Turk, and F. Gubensek Serine proteinase inhibitors from Viper ammodytes venom. Isolation and kinetic studies Eur. J. Biochem. 133 1983 427 432
    • (1983) Eur. J. Biochem. , vol.133 , pp. 427-432
    • Ritonja, A.1    Turk, V.2    Gubensek, F.3
  • 4
    • 0020665525 scopus 로고
    • Complete amino acid sequences of two protease inhibitors in the venom of Bungarus fasciatus
    • C.S. Liu, T.C. Wu, and T.B. Lo Complete amino acid sequences of two protease inhibitors in the venom of Bungarus fasciatus Int. J. Pept. Protein Res. 21 1983 209 215
    • (1983) Int. J. Pept. Protein Res. , vol.21 , pp. 209-215
    • Liu, C.S.1    Wu, T.C.2    Lo, T.B.3
  • 5
    • 0020964438 scopus 로고
    • The primary structure of Vipera ammodytes venom chymotrypsin inhibitor
    • A. Ritonja, B. Meloun, and F. Gubensek The primary structure of Vipera ammodytes venom chymotrypsin inhibitor Biochim. Biophys. Acta 746 1983 138 145
    • (1983) Biochim. Biophys. Acta , vol.746 , pp. 138-145
    • Ritonja, A.1    Meloun, B.2    Gubensek, F.3
  • 6
    • 0025080866 scopus 로고
    • Purification and characterization of a chymotrypsin Kunitz inhibitor type of polypeptide from the venom of cobra (Naja naja naja)
    • J. Shafqat, Z.H. Zaidi, and H. Jornvall Purification and characterization of a chymotrypsin Kunitz inhibitor type of polypeptide from the venom of cobra (Naja naja naja) FEBS Lett. 275 1990 6 8
    • (1990) FEBS Lett. , vol.275 , pp. 6-8
    • Shafqat, J.1    Zaidi, Z.H.2    Jornvall, H.3
  • 7
    • 0025648592 scopus 로고
    • Primary structure and functional properties of cobra (Naja naja naja) venom Kunitz-type trypsin inhibitor
    • J. Shafqat, O.U. Beg, S.J. Yin, Z.H. Zaidi, and H. Jornvall Primary structure and functional properties of cobra (Naja naja naja) venom Kunitz-type trypsin inhibitor Eur. J. Biochem. 194 1990 337 341
    • (1990) Eur. J. Biochem. , vol.194 , pp. 337-341
    • Shafqat, J.1    Beg, O.U.2    Yin, S.J.3    Zaidi, Z.H.4    Jornvall, H.5
  • 8
    • 0025937275 scopus 로고
    • Purification and characterization of a Kunitz-type trypsin inhibitor from Leaf-nosed viper venom
    • A.R. Siddigi, Z.H. Zaidi, and H. Jornvall Purification and characterization of a Kunitz-type trypsin inhibitor from Leaf-nosed viper venom FEBS Lett. 294 1991 141 143
    • (1991) FEBS Lett. , vol.294 , pp. 141-143
    • Siddigi, A.R.1    Zaidi, Z.H.2    Jornvall, H.3
  • 9
    • 0019018299 scopus 로고
    • Snake venoms. The amino acid sequences of two proteinase inhibitor homologues from Dendroaspis angusticeps venom
    • F.J. Joubert, and N. Taljaard Snake venoms. The amino acid sequences of two proteinase inhibitor homologues from Dendroaspis angusticeps venom Hoppe-Seyler Z. Physiol. Chem. 361 1980 661 674
    • (1980) Hoppe-Seyler Z. Physiol. Chem. , vol.361 , pp. 661-674
    • Joubert, F.J.1    Taljaard, N.2
  • 10
    • 0017848728 scopus 로고
    • Snake venoms. The amino-acid sequence of trypsin inhibitor e of Dendroaspis polylepis polylepis (Black Mamba) venom
    • F.L. Joubert, and D.J. Strydom Snake venoms. The amino-acid sequence of trypsin inhibitor E of Dendroaspis polylepis polylepis (Black Mamba) venom Eur. J. Biochem. 87 1978 191 198
    • (1978) Eur. J. Biochem. , vol.87 , pp. 191-198
    • Joubert, F.L.1    Strydom, D.J.2
  • 11
    • 0002443106 scopus 로고
    • Dendrotoxins: Snake toxins that block potassium channels and facilitate neurotransmitter release
    • A.L. Harvey Pergamon Press New York
    • A.L. Harvey, and A.J. Anderson Dendrotoxins: snake toxins that block potassium channels and facilitate neurotransmitter release A.L. Harvey Snake Toxins 1991 Pergamon Press New York 131 164
    • (1991) Snake Toxins , pp. 131-164
    • Harvey, A.L.1    Anderson, A.J.2
  • 13
    • 0033613817 scopus 로고    scopus 로고
    • Evolutionary trace analysis of Kunitz/BPTI family of proteins: Functional divergence may have been based on confomational adjustment
    • L. Pritchard, and M.J. Dufton Evolutionary trace analysis of Kunitz/BPTI family of proteins: functional divergence may have been based on confomational adjustment J. Mol. Biol. 285 1999 1589 1607
    • (1999) J. Mol. Biol. , vol.285 , pp. 1589-1607
    • Pritchard, L.1    Dufton, M.J.2
  • 14
    • 0035977002 scopus 로고    scopus 로고
    • Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the Elapid snake Bungarus fasciatus
    • C. Chen, C.H. Hsu, N.Y. Sun, Y.C. Lin, S.H. Chiou, and S.H. Wu Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the Elapid snake Bungarus fasciatus J. Biol. Chem. 276 2001 45079 45087
    • (2001) J. Biol. Chem. , vol.276 , pp. 45079-45087
    • Chen, C.1    Hsu, C.H.2    Sun, N.Y.3    Lin, Y.C.4    Chiou, S.H.5    Wu, S.H.6
  • 17
    • 0033612211 scopus 로고    scopus 로고
    • Interscaffolding additivity: Binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteases
    • D. Krowarsch, M. Dadlez, O. Buczek, I. Krokoszynska, A.O. Smalas, and J. Otlewski Interscaffolding additivity: binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteases J. Mol. Biol. 289 1999 175 186
    • (1999) J. Mol. Biol. , vol.289 , pp. 175-186
    • Krowarsch, D.1    Dadlez, M.2    Buczek, O.3    Krokoszynska, I.4    Smalas, A.O.5    Otlewski, J.6
  • 18
    • 0034721778 scopus 로고    scopus 로고
    • Inhibition of six serine proteinases of the human coagulation system by mutants of bovine pancreatic trypsin inhibitor
    • A. Crzesiak, I. Krokoszynska, D. Krowarsch, O. Buczek, M. Dadlez, and J. Otlewski Inhibition of six serine proteinases of the human coagulation system by mutants of bovine pancreatic trypsin inhibitor J. Biol. Chem. 275 2000 33346 33352
    • (2000) J. Biol. Chem. , vol.275 , pp. 33346-33352
    • Crzesiak, A.1    Krokoszynska, I.2    Krowarsch, D.3    Buczek, O.4    Dadlez, M.5    Otlewski, J.6
  • 19
    • 0034604364 scopus 로고    scopus 로고
    • Substitutions at the P1 position in BPTI strongly affect the association energy with serine proteases
    • A. Grzesiak, R. Helland, A.O. Smalas, D. Krowarsch, M. Dadlez, and J. Otlewski Substitutions at the P1 position in BPTI strongly affect the association energy with serine proteases J. Mol. Biol. 301 2000 205 217
    • (2000) J. Mol. Biol. , vol.301 , pp. 205-217
    • Grzesiak, A.1    Helland, R.2    Smalas, A.O.3    Krowarsch, D.4    Dadlez, M.5    Otlewski, J.6
  • 20
    • 0031046939 scopus 로고    scopus 로고
    • Foci of amino acid residue conservation in the 3D structures of the Kunitz/BPTI proteinase inhibitors: How do variants from snake venom differ?
    • L. Cardle, and M.J. Dufton Foci of amino acid residue conservation in the 3D structures of the Kunitz/BPTI proteinase inhibitors: how do variants from snake venom differ? Protein Eng. 10 1997 131 136
    • (1997) Protein Eng. , vol.10 , pp. 131-136
    • Cardle, L.1    Dufton, M.J.2
  • 21
    • 0028982743 scopus 로고
    • 2-bungarotoxin: Potassium channel binding by Kunitz modules and targeted phospholipase action
    • 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action Structure 3 1995 1109 1119
    • (1995) Structure , vol.3 , pp. 1109-1119
    • Kwong, P.D.1    McDonald, N.Q.2    Sigler, P.B.3    Hendrickson, W.A.4
  • 22
    • 0032528860 scopus 로고    scopus 로고
    • Cloning and functional expression of B chains of β-bungarotoxin from Bungarus multicinctus (Taiwan banded krait)
    • P.F. Wu, S.N. Wu, C.C. Chang, and L.S. Chang Cloning and functional expression of B chains of β-bungarotoxin from Bungarus multicinctus (Taiwan banded krait) Biochem. J. 334 1998 87 92
    • (1998) Biochem. J. , vol.334 , pp. 87-92
    • Wu, P.F.1    Wu, S.N.2    Chang, C.C.3    Chang, L.S.4
  • 23
    • 0030598859 scopus 로고    scopus 로고
    • 2 in Escherichia coli, a full active enzyme generated by hydrolyzing with aminopeptidase
    • 2 in Escherichia coli, a full active enzyme generated by hydrolyzing with aminopeptidase Biochem. Biophys. Res. Commun. 225 1996 990 996
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 990-996
    • Chang, L.S.1    Wu, P.F.2    Chang, C.C.3
  • 24
    • 0034805614 scopus 로고    scopus 로고
    • Purification and characterization of a chymotrypsin inhibitor from the venom of Ophiophagus hannah (King cobra)
    • L.S. Chang, C. Chung, S.B. Huang, and S.R. Lin Purification and characterization of a chymotrypsin inhibitor from the venom of Ophiophagus hannah (King cobra) Biochem. Biophys. Res. Commun. 283 2001 862 867
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 862-867
    • Chang, L.S.1    Chung, C.2    Huang, S.B.3    Lin, S.R.4
  • 25
    • 0031447137 scopus 로고    scopus 로고
    • A novel neurotoxin, cobrotoxin b, from Naja naja atra (Taiwan cobra) venom: Purification, characterization and gene organization
    • L.S. Chang, Y.C. Chou, S.R. Lin, B.N. Wu, J. Lin, E. Hong, Y.J. Sun, and C.D. Hsiao A novel neurotoxin, cobrotoxin b, from Naja naja atra (Taiwan cobra) venom: purification, characterization and gene organization J. Biochem. 122 1997 1252 1259
    • (1997) J. Biochem. , vol.122 , pp. 1252-1259
    • Chang, L.S.1    Chou, Y.C.2    Lin, S.R.3    Wu, B.N.4    Lin, J.5    Hong, E.6    Sun, Y.J.7    Hsiao, C.D.8
  • 26
    • 0033863759 scopus 로고    scopus 로고
    • Genetic organization of a chain and B chain of β-bungarotoxin from Taiwan banded krait (Bungarus multicinctus). A chain genes and B chain genes do not share a common origin
    • P.F. Wu, and L.S. Chang Genetic organization of A chain and B chain of β-bungarotoxin from Taiwan banded krait (Bungarus multicinctus). A chain genes and B chain genes do not share a common origin Eur. J. Biochem. 267 2000 4668 4675
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4668-4675
    • Wu, P.F.1    Chang, L.S.2
  • 28
    • 0038643710 scopus 로고    scopus 로고
    • Adaptive evolution in the snake venom Kunitz/BPTI protein family
    • V. Zupunski, D. Kordis, and F. Gubensek Adaptive evolution in the snake venom Kunitz/BPTI protein family FEBS Lett. 547 2003 131 136
    • (2003) FEBS Lett. , vol.547 , pp. 131-136
    • Zupunski, V.1    Kordis, D.2    Gubensek, F.3
  • 29
    • 0015901579 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region
    • A. Ruhlmann, D. Kukla, P. Schwager, K. Bartels, and R. Huber Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region J. Mol. Biol. 77 1973 417 436
    • (1973) J. Mol. Biol. , vol.77 , pp. 417-436
    • Ruhlmann, A.1    Kukla, D.2    Schwager, P.3    Bartels, K.4    Huber, R.5
  • 30
    • 0026677581 scopus 로고
    • Site-directed analysis of the functional domains in the factor Xa inhibitor tick anticoagulant peptide: Identification of two distinct regions that constitute the enzyme recognition sites
    • C.T. Dunwiddie, P.K. Neeper, E.M. Nutt, L. Waxman, D.E. Smith, K.J. Hofmann, P.K. Lumma, V.M. Garsky, and G.P. Vlasuk Site-directed analysis of the functional domains in the factor Xa inhibitor tick anticoagulant peptide: identification of two distinct regions that constitute the enzyme recognition sites Biochemistry 31 1992 12126 12131
    • (1992) Biochemistry , vol.31 , pp. 12126-12131
    • Dunwiddie, C.T.1    Neeper, P.K.2    Nutt, E.M.3    Waxman, L.4    Smith, D.E.5    Hofmann, K.J.6    Lumma, P.K.7    Garsky, V.M.8    Vlasuk, G.P.9
  • 31
    • 0032922732 scopus 로고    scopus 로고
    • Postsynaptic α-neurotoxin gene of the spitting cobra, Naja naja sputatrix: Structure, organization, and phylogenetic analysis
    • F. Afifiyan, A. Armugam, C.H. Tan, P. Gopalakrishnakone, and K. Jeyaseelan Postsynaptic α-neurotoxin gene of the spitting cobra, Naja naja sputatrix: structure, organization, and phylogenetic analysis Genome Res. 9 1999 259 266
    • (1999) Genome Res. , vol.9 , pp. 259-266
    • Afifiyan, F.1    Armugam, A.2    Tan, C.H.3    Gopalakrishnakone, P.4    Jeyaseelan, K.5
  • 32
    • 0033570288 scopus 로고    scopus 로고
    • Genetic organization of α-bungarotoxins from Bungarus multicinctus (Taiwan banded krait): Evidence showing that the production of α-bungarotoxin isotoxins are not derived from edited mRNAs
    • L.S. Chang, S.K. Lin, S.B. Huang, and M. Hsiao Genetic organization of α-bungarotoxins from Bungarus multicinctus (Taiwan banded krait): evidence showing that the production of α-bungarotoxin isotoxins are not derived from edited mRNAs Nucleic Acids Res. 27 1999 3970 3975
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3970-3975
    • Chang, L.S.1    Lin, S.K.2    Huang, S.B.3    Hsiao, M.4
  • 33
    • 0031869367 scopus 로고    scopus 로고
    • Structure and organization of the polymorphic cardiotoxin gene in Naja naja sputatrix
    • R. Lachumanan, A. Armugam, C.H. Tan, and K. Jeyaseelan Structure and organization of the polymorphic cardiotoxin gene in Naja naja sputatrix FEBS Lett. 433 1998 119 124
    • (1998) FEBS Lett. , vol.433 , pp. 119-124
    • Lachumanan, R.1    Armugam, A.2    Tan, C.H.3    Jeyaseelan, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.