메뉴 건너뛰기




Volumn 45, Issue 5, 2005, Pages 571-580

Primary structure of brevilysin L4, an enzymatically active fragment of a disintegrin precursor from Gloydius halys brevicaudus venom

Author keywords

Autoproteolysis; Disintegrin precursor; Gloydius halys brevicaudus; Metalloproteinase; Primary structure; Snake venom

Indexed keywords

BREVICAUDIN 1; BREVILYSIN L 4; CALCIUM ION; DISINTEGRIN; METALLOPROTEINASE; PEPTIDE FRAGMENT; POLYPEPTIDE; SNAKE VENOM; UNCLASSIFIED DRUG; ZINC;

EID: 15044354001     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2004.12.005     Document Type: Article
Times cited : (3)

References (33)
  • 1
    • 0026348765 scopus 로고
    • A common precursor of a putative hemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhodostoma: Molecular cloning and sequence analysis
    • L.-C. Au, Y.-B. Huang, T.-F. Huang, G.-W. Teh, H.-H. Lin, and K.-B. Choo A common precursor of a putative hemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhodostoma: molecular cloning and sequence analysis Biochem. Biophys. Res. Commun. 181 1991 585 593
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 585-593
    • Au, L.-C.1    Huang, Y.-B.2    Huang, T.-F.3    Teh, G.-W.4    Lin, H.-H.5    Choo, K.-B.6
  • 2
    • 0018799146 scopus 로고
    • Manual solid phase sequence analysis of polypeptides using 4-N,N-dimethylaminoazobenzene 4′-isothiocyanate
    • T.-Y. Chang Manual solid phase sequence analysis of polypeptides using 4-N,N-dimethylaminoazobenzene 4′-isothiocyanate Biochim. Biophys. Acta 578 1979 188 195
    • (1979) Biochim. Biophys. Acta , vol.578 , pp. 188-195
    • Chang, T.-Y.1
  • 3
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • P. Chomczynski, and N. Sacchi Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction Anal. Biochem. 162 1987 156 159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 4
    • 0022497628 scopus 로고
    • Substrate specificities and inhibition of two hemorrhagic zinc proteases Ht-c and Ht-d from Crotalus atrox venom
    • J.W. Fox, R. Campbell, L. Beggerly, and J.B. Bjarnason Substrate specificities and inhibition of two hemorrhagic zinc proteases Ht-c and Ht-d from Crotalus atrox venom Eur. J. Biochem. 156 1986 65 72
    • (1986) Eur. J. Biochem. , vol.156 , pp. 65-72
    • Fox, J.W.1    Campbell, R.2    Beggerly, L.3    Bjarnason, J.B.4
  • 5
    • 0014939933 scopus 로고
    • The chromatographic determination of cystine and cysteine residues in proteins as s-β-(4-pyridylethyl)cysteine
    • M. Friedman, L.H. Krull, and J.F. Cavins The chromatographic determination of cystine and cysteine residues in proteins as s-β-(4-pyridylethyl)cysteine J. Biol. Chem. 245 1970 3671 3868
    • (1970) J. Biol. Chem. , vol.245 , pp. 3671-3868
    • Friedman, M.1    Krull, L.H.2    Cavins, J.F.3
  • 6
    • 0028836750 scopus 로고
    • Purification and characterization of a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom
    • S. Fujimura, T. Rikimaru, S. Baba, J. Hori, X.-Q. Hao, S. Terada, and E. Kimoto Purification and characterization of a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom Biochim. Biophys. Acta 1243 1995 94 100
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 94-100
    • Fujimura, S.1    Rikimaru, T.2    Baba, S.3    Hori, J.4    Hao, X.-Q.5    Terada, S.6    Kimoto, E.7
  • 7
    • 0033850683 scopus 로고    scopus 로고
    • Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus
    • S. Fujimura, K. Oshikawa, S. Terada, and E. Kimoto Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus J. Biohem. 128 2000 167 173
    • (2000) J. Biohem. , vol.128 , pp. 167-173
    • Fujimura, S.1    Oshikawa, K.2    Terada, S.3    Kimoto, E.4
  • 9
    • 0032582674 scopus 로고    scopus 로고
    • Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus
    • W. Gong, X. Zhu, S. Liu, M. Teng, and L. Niu Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus J. Mol. Biol. 283 1998 657 668
    • (1998) J. Mol. Biol. , vol.283 , pp. 657-668
    • Gong, W.1    Zhu, X.2    Liu, S.3    Teng, M.4    Niu, L.5
  • 10
    • 0026748687 scopus 로고
    • Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: Evidence for signal, zymogen, and disintegrin-like structures
    • L.A. Hite, J.D. Shannon, J.B. Bjarnason, and J.W. Fox Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: evidence for signal, zymogen, and disintegrin-like structures Biochemistry 31 1992 6203 6211
    • (1992) Biochemistry , vol.31 , pp. 6203-6211
    • Hite, L.A.1    Shannon, J.D.2    Bjarnason, J.B.3    Fox, J.W.4
  • 11
    • 0028337108 scopus 로고
    • CDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins
    • L.A. Hite, L.G. Jia, J.B. Bjarnason, and J.W. Fox cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins Arch. Biochem. Biophys. 308 1994 182 191
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L.G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 13
    • 0025799478 scopus 로고
    • The origin of matrix metalloproteinases and their familiar relationship
    • G.J.P. Murphy, G. Murphy, and J.J. Reynolds The origin of matrix metalloproteinases and their familiar relationship FEBS Lett. 289 1991 4 7
    • (1991) FEBS Lett. , vol.289 , pp. 4-7
    • Murphy, G.J.P.1    Murphy, G.2    Reynolds, J.J.3
  • 14
    • 0025365318 scopus 로고
    • Sequence of a cDNA encoding the platelet aggregation inhibitor trigramin
    • M.P. Neeper, and M.A. Jacobson Sequence of a cDNA encoding the platelet aggregation inhibitor trigramin Nucleic Acids Res. 18 1990 4255
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4255
    • Neeper, M.P.1    Jacobson, M.A.2
  • 15
    • 0037016015 scopus 로고    scopus 로고
    • A new gene structure of the disintegrin family: A subunit of dimeric disintegrin has a short coding region
    • D. Okuda, H. Koike, and T. Morita A new gene structure of the disintegrin family: a subunit of dimeric disintegrin has a short coding region Biochemistry 41 2002 14248 14254
    • (2002) Biochemistry , vol.41 , pp. 14248-14254
    • Okuda, D.1    Koike, H.2    Morita, T.3
  • 16
    • 15044361501 scopus 로고    scopus 로고
    • Isolation and primary structures of platelet aggregation inhibitors from Gloydius halys brevicaudus venom
    • K. Oshikawa, Y. Yasukouchi, and S. Terada Isolation and primary structures of platelet aggregation inhibitors from Gloydius halys brevicaudus venom Fukuoka Univ. Sci. Rep. 30 2000 201 208
    • (2000) Fukuoka Univ. Sci. Rep. , vol.30 , pp. 201-208
    • Oshikawa, K.1    Yasukouchi, Y.2    Terada, S.3
  • 17
    • 0020632120 scopus 로고
    • Potent platelet aggregation inhibitor from Trimeresurus gramineus snake venom
    • C. Ouyang, and T.F. Huang Potent platelet aggregation inhibitor from Trimeresurus gramineus snake venom Biochim. Biophys. Acta 757 1983 332 341
    • (1983) Biochim. Biophys. Acta , vol.757 , pp. 332-341
    • Ouyang, C.1    Huang, T.F.2
  • 18
    • 0027081926 scopus 로고
    • Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom
    • A. Randolph, S.H. Chamverlain, H.-L.C. Chu, A.D. Retzios, F.S. Markland Jr., and F.R. Masiarz Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom Protein Sci. 1 1992 590 600
    • (1992) Protein Sci. , vol.1 , pp. 590-600
    • Randolph, A.1    Chamverlain, S.H.2    Chu, H.-L.C.3    Retzios, A.D.4    Markland Jr., F.S.5    Masiarz, F.R.6
  • 19
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • A.J. Barrett Academic Press New York
    • N.D. Rawlings, and A.J. Barrett Evolutionary families of metallopeptidases A.J. Barrett Methods in Enzymology vol. 248 1995 Academic Press New York 183 228
    • (1995) Methods in Enzymology , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 20
    • 0029020526 scopus 로고
    • Molecular cloning and sequence analysis of cDNAs for metalloproteinases from broad-banded copperhead Agkistrodon contortrix laticinctus
    • H.S. Selistre de Araujo, and C.L. Ownby Molecular cloning and sequence analysis of cDNAs for metalloproteinases from broad-banded copperhead Agkistrodon contortrix laticinctus Arch. Biochem. Biophys. 320 1995 141 148
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 141-148
    • Selistre De Araujo, H.S.1    Ownby, C.L.2
  • 21
    • 0001572034 scopus 로고    scopus 로고
    • Expression, activation, and processing of the recombinant snake venom metalloproteinase, pro-atrolysin e
    • K. Shimokawa, L.-G. Jia, S.-M. Wang, and J.W. Fox Expression, activation, and processing of the recombinant snake venom metalloproteinase, pro-atrolysin E Arch. Biochem. Biophys. 335 1996 283 294
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 283-294
    • Shimokawa, K.1    Jia, L.-G.2    Wang, S.-M.3    Fox, J.W.4
  • 22
    • 0028969678 scopus 로고
    • The metzincins: Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • W. Stocker, F. Grams, U. Baumann, P. Reinemer, F.X. Gomis-Rüth, D.B. McKay, and W. Bode The metzincins: topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases Protein Sci. 4 1995 823 840
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Rüth, F.X.5    McKay, D.B.6    Bode, W.7
  • 23
    • 0024690967 scopus 로고
    • 2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the Habu snake, Trimeresurus flavoviridis
    • 2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the Habu snake, Trimeresurus flavoviridis J. Biochem. 106 1989 151 157
    • (1989) J. Biochem. , vol.106 , pp. 151-157
    • Takeya, H.1    Arakawa, M.2    Iwanaga, S.3    Omori-Satoh, T.4
  • 24
    • 0024997837 scopus 로고
    • The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis
    • H. Takeya, K. Oda, T. Miyata, T. Omori-Satoh, and S. Iwanaga The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis J. Biol. Chem. 265 1990 16068 16073
    • (1990) J. Biol. Chem. , vol.265 , pp. 16068-16073
    • Takeya, H.1    Oda, K.2    Miyata, T.3    Omori-Satoh, T.4    Iwanaga, S.5
  • 25
    • 0027193420 scopus 로고
    • Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes
    • H. Takeya, S. Nishida, N. Nishino, Y. Makinose, T. Omori-Satoh, T. Nikai, H. Sugihara, and S. Iwanaga Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes J. Biochem. 113 1993 473 483
    • (1993) J. Biochem. , vol.113 , pp. 473-483
    • Takeya, H.1    Nishida, S.2    Nishino, N.3    Makinose, Y.4    Omori-Satoh, T.5    Nikai, T.6    Sugihara, H.7    Iwanaga, S.8
  • 26
    • 0033014355 scopus 로고    scopus 로고
    • Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom
    • S. Terada, J. Hori, S. Fujimura, and E. Kimoto Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom J. Biochem. 125 1999 64 69
    • (1999) J. Biochem. , vol.125 , pp. 64-69
    • Terada, S.1    Hori, J.2    Fujimura, S.3    Kimoto, E.4
  • 27
    • 15044348686 scopus 로고    scopus 로고
    • 2 with platelet aggregation inhibitory activity from the venom of Agkistrodon ussuriensis
    • 2 with platelet aggregation inhibitory activity from the venom of Agkistrodon ussuriensis Fukuoka Univ. Sci. Rep. 29 1999 119 126
    • (1999) Fukuoka Univ. Sci. Rep. , vol.29 , pp. 119-126
    • Terada, S.1    Ichihara, M.2    Oshikawa, K.3    Noda, S.4
  • 28
    • 0021531735 scopus 로고
    • New fluorogenic reagent having halogenobenzofurazan structure for thiols: 4-(aminosulfony)-7-fluoro-2,1,3-benzoxadiazole
    • T. Toyo'oka, and K. Imai New fluorogenic reagent having halogenobenzofurazan structure for thiols: 4-(aminosulfony)-7-fluoro-2,1,3- benzoxadiazole Anal. Chem. 56 1984 2461 2464
    • (1984) Anal. Chem. , vol.56 , pp. 2461-2464
    • Toyo'Oka, T.1    Imai, K.2
  • 29
    • 0021738226 scopus 로고
    • Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes
    • S.S. Twining Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes Anal. Biochem. 143 1984 30 34
    • (1984) Anal. Biochem. , vol.143 , pp. 30-34
    • Twining, S.S.1
  • 30
    • 0028233804 scopus 로고
    • A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet aggregation
    • Y. Usami, Y. Fujimura, S. Miura, H. Shima, E. Yoshida, A. Yoshioka, K. Hirano, M. Suzuki, and K. Titani A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet aggregation Biochem. Biophys. Res. Commun. 201 1994 331 339
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 331-339
    • Usami, Y.1    Fujimura, Y.2    Miura, S.3    Shima, H.4    Yoshida, E.5    Yoshioka, A.6    Hirano, K.7    Suzuki, M.8    Titani, K.9
  • 31
    • 0025398721 scopus 로고
    • What if: A molecular modeling and drug design program
    • G. Vriend what if: a molecular modeling and drug design program J. Mol. Graph. 8 1990 52 56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 32
    • 0032981072 scopus 로고    scopus 로고
    • Nucleotide sequence of a cDNA encoding a common precursor of disintegrin flavostatin and hemorrhagic factor HR2a from the venom of Trimeresurus flavoviridis
    • D. Yamada, Y. Shin, and T. Morita Nucleotide sequence of a cDNA encoding a common precursor of disintegrin flavostatin and hemorrhagic factor HR2a from the venom of Trimeresurus flavoviridis FEBS Lett. 451 1999 299 302
    • (1999) FEBS Lett. , vol.451 , pp. 299-302
    • Yamada, D.1    Shin, Y.2    Morita, T.3
  • 33
    • 0023241667 scopus 로고
    • Purification, characterization and substrate specificity of a basic proteinase in the venom of Habu (Trimeresurus flavoviridis)
    • Y. Yamakawa, T. Omori-Satoh, and S. Sadahiro Purification, characterization and substrate specificity of a basic proteinase in the venom of Habu (Trimeresurus flavoviridis) Biochim. Biophys. Acta 925 1987 124 132
    • (1987) Biochim. Biophys. Acta , vol.925 , pp. 124-132
    • Yamakawa, Y.1    Omori-Satoh, T.2    Sadahiro, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.