메뉴 건너뛰기




Volumn 82, Issue 3, 2000, Pages 251-257

The role of tryptophan residues in the hemolytic activity of stonustoxin, a lethal factor from stonefish (Synanceja horrida) venom

Author keywords

[No Author keywords available]

Indexed keywords

FISH VENOM; STONUSTOXIN; TRYPTOPHAN;

EID: 0034117834     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(00)00203-0     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 0025775633 scopus 로고
    • Purification and partial characterisation of stonustoxin (lethal factor) from Synanceja horrida venom
    • Poh C.H., Yuen R., Khoo H.E., Chung M., Gwee M., Gopalakrishnakone P. Purification and partial characterisation of stonustoxin (lethal factor) from Synanceja horrida venom. Comp. Biochem. Physiol. 99B:1991;793-798.
    • (1991) Comp. Biochem. Physiol. , vol.99 , pp. 793-798
    • Poh, C.H.1    Yuen, R.2    Khoo, H.E.3    Chung, M.4    Gwee, M.5    Gopalakrishnakone, P.6
  • 2
    • 0027019410 scopus 로고
    • Biological activities of Synanceja horrida (stonefish) venom
    • Khoo H.E., Yuen R., Poh C.H., Tan C.H. Biological activities of Synanceja horrida (stonefish) venom. Nat. Toxins. 1:1992;54-60.
    • (1992) Nat. Toxins , vol.1 , pp. 54-60
    • Khoo, H.E.1    Yuen, R.2    Poh, C.H.3    Tan, C.H.4
  • 5
    • 0030796817 scopus 로고    scopus 로고
    • Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom. Pore-formation and the role of cationic amino acid residues
    • Chen D., Kini R.M., Yuen R., Khoo H.E. Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom. Pore-formation and the role of cationic amino acid residues. Biochem. J. 325:1997;685-691.
    • (1997) Biochem. J. , vol.325 , pp. 685-691
    • Chen, D.1    Kini, R.M.2    Yuen, R.3    Khoo, H.E.4
  • 6
    • 17344378549 scopus 로고    scopus 로고
    • Role of free thiol groups in the biological activities of stonustoxin, a lethal factor from stonefish (Synanceja horrida) venom
    • Khoo H.E., Chen D., Yuen R. Role of free thiol groups in the biological activities of stonustoxin, a lethal factor from stonefish (Synanceja horrida) venom. Toxicon. 36:1998;469-478.
    • (1998) Toxicon , vol.36 , pp. 469-478
    • Khoo, H.E.1    Chen, D.2    Yuen, R.3
  • 7
    • 0025843497 scopus 로고
    • Detection of a cytolytic toxin in the venom of the stonefish (Synanceja trachynis)
    • Kreger A.S. Detection of a cytolytic toxin in the venom of the stonefish (Synanceja trachynis). Toxicon. 29:1991;733-743.
    • (1991) Toxicon , vol.29 , pp. 733-743
    • Kreger, A.S.1
  • 8
    • 21144475769 scopus 로고
    • Properties of a lethal factor in stonefish Synanceja verrucosa venom
    • Shiomi K., Hosaka M., Kituchi T. Properties of a lethal factor in stonefish Synanceja verrucosa venom. Nippon Suis. Gakk. 59:1993;1099-1103.
    • (1993) Nippon Suis. Gakk. , vol.59 , pp. 1099-1103
    • Shiomi, K.1    Hosaka, M.2    Kituchi, T.3
  • 9
    • 0028960998 scopus 로고
    • Enzymatic properties of the stonefish (Synanceja verrucosa) venom and purification of a lethal, hypotensive and cytolytic factor
    • Garnier P., Goudey-Perriere F., Breton P., Dewulf C., Peter F., Perriere C. Enzymatic properties of the stonefish (Synanceja verrucosa) venom and purification of a lethal, hypotensive and cytolytic factor. Toxicon. 33:1995;143-155.
    • (1995) Toxicon , vol.33 , pp. 143-155
    • Garnier, P.1    Goudey-Perriere, F.2    Breton, P.3    Dewulf, C.4    Peter, F.5    Perriere, C.6
  • 10
    • 0025761657 scopus 로고
    • Cytolytic pore-forming proteins and peptides: Is there a common structural motif?
    • Ojcius D.M., Young J.D. Cytolytic pore-forming proteins and peptides: is there a common structural motif? TIBS. 16:1991;225-229.
    • (1991) TIBS , vol.16 , pp. 225-229
    • Ojcius, D.M.1    Young, J.D.2
  • 12
    • 0024461439 scopus 로고
    • A common cytolytic region in myotoxins, hemolysins, cardiotoxins and antibacterial peptides
    • Kini R.M., Evans H.J. A common cytolytic region in myotoxins, hemolysins, cardiotoxins and antibacterial peptides. Int. J. Pept. Protein Res. 34:1989;277-286.
    • (1989) Int. J. Pept. Protein Res. , vol.34 , pp. 277-286
    • Kini, R.M.1    Evans, H.J.2
  • 13
    • 0025894727 scopus 로고
    • Tryptophan 65 is essential for hemolytic activity of the thermostable direct hemolysin from Vibrio parahaemolyticus
    • Toda H., Sakiyama F., Yoh M., Honda T., Miwatani T. Tryptophan 65 is essential for hemolytic activity of the thermostable direct hemolysin from Vibrio parahaemolyticus. Toxicon. 29:1991;837-844.
    • (1991) Toxicon , vol.29 , pp. 837-844
    • Toda, H.1    Sakiyama, F.2    Yoh, M.3    Honda, T.4    Miwatani, T.5
  • 14
    • 0029972377 scopus 로고    scopus 로고
    • Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin
    • Sekino S.N., Nakamura M., Mitsui K.I., Ohno I.Y. Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin. Eur. J. Biochem. 241:1996;941-947.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 941-947
    • Sekino, S.N.1    Nakamura, M.2    Mitsui, K.I.3    Ohno, I.Y.4
  • 15
    • 0030245816 scopus 로고    scopus 로고
    • Structural requirements for the edema-inducing and hemolytic activities of mastoparan B isolated from the hornet (Vespa basalis) venom
    • Ho C.L., Lin Y.L., Chen W.C., Hwang L.L., Yu H.M., Wang K.T. Structural requirements for the edema-inducing and hemolytic activities of mastoparan B isolated from the hornet (Vespa basalis) venom. Toxicon. 34:1996;1027-1035.
    • (1996) Toxicon , vol.34 , pp. 1027-1035
    • Ho, C.L.1    Lin, Y.L.2    Chen, W.C.3    Hwang, L.L.4    Yu, H.M.5    Wang, K.T.6
  • 16
    • 0025717603 scopus 로고
    • Probing the relationships between the structure and hemolytic activity of melittin with a complete set of leucine substitution analogs
    • Blondelle S.E., Houghten R.A. Probing the relationships between the structure and hemolytic activity of melittin with a complete set of leucine substitution analogs. Pept. Res. 4:1991;12-18.
    • (1991) Pept. Res. , vol.4 , pp. 12-18
    • Blondelle, S.E.1    Houghten, R.A.2
  • 18
    • 0026516947 scopus 로고
    • The role of tryptophan in structural and functional properties of equinatoxin II
    • Turk T., Macek P., Gubensek F. The role of tryptophan in structural and functional properties of equinatoxin II. Biochim. Biophys. Acta. 1119:1992;1-4.
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 1-4
    • Turk, T.1    MacEk, P.2    Gubensek, F.3
  • 19
    • 0031575823 scopus 로고    scopus 로고
    • Stimulation of haemolytic activity of sea anemone cytolysins by 8-anilino-1-naphthalenesulphonate
    • Khoo H.E., Fong C.L., Yuen R., Chen D. Stimulation of haemolytic activity of sea anemone cytolysins by 8-anilino-1-naphthalenesulphonate. Biochem. Biophys. Res. Commun. 232:1997;422-426.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 422-426
    • Khoo, H.E.1    Fong, C.L.2    Yuen, R.3    Chen, D.4
  • 20
    • 0026459655 scopus 로고
    • Role of Tyr and Trp in membrane responses of Pyrularia thionin determined by optical and NMR spectra following Tyr iodination and Trp modification
    • Fracki W.S., Li D., Owen N., Perry C., Naisbitt G.H., Vernon L.P. Role of Tyr and Trp in membrane responses of Pyrularia thionin determined by optical and NMR spectra following Tyr iodination and Trp modification. Toxicon. 30:1992;1427-1440.
    • (1992) Toxicon , vol.30 , pp. 1427-1440
    • Fracki, W.S.1    Li, D.2    Owen, N.3    Perry, C.4    Naisbitt, G.H.5    Vernon, L.P.6
  • 21
    • 0024963570 scopus 로고
    • Conformational states of beta-lactamase: Molten-globule states at acidic and alkaline pH with high salt
    • Goto Y., Fink A.L. Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt. Biochemistry. 28:1989;945-952.
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 22
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1'-bis (4-anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
    • Shi L., Palleros D.R., Fink A.L. Protein conformational changes induced by 1,1'-bis (4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry. 33:1994;7536-7546.
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 23
    • 0029115374 scopus 로고
    • Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates
    • Engelhard M., Evans P.A. Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates. Prot. Sci. 4:1995;1553-1562.
    • (1995) Prot. Sci. , vol.4 , pp. 1553-1562
    • Engelhard, M.1    Evans, P.A.2
  • 24
    • 0013916008 scopus 로고
    • The reactivity toward N-bromosuccinimide of tryptophan in enzymes, zymogens, and inhibited enzymes
    • Spande T.F., Green N.M., Witkop B. The reactivity toward N-bromosuccinimide of tryptophan in enzymes, zymogens, and inhibited enzymes. Biochemistry. 5:1966;1926-1933.
    • (1966) Biochemistry , vol.5 , pp. 1926-1933
    • Spande, T.F.1    Green, N.M.2    Witkop, B.3
  • 25
    • 0022503457 scopus 로고
    • H.W. Hirs, Timasheff S.N. London and New York: Academic Press
    • Yang J.T., Wu C.S.C., Martinez H.M. Hirs C.H.W, Timasheff S.N. Methods in Enzymology. Vol. 130:1986;208 Academic Press, London and New York.
    • (1986) Methods in Enzymology , vol.130 , pp. 208
    • Yang, J.T.1    Wu, C.S.C.2    Martinez, H.M.3
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0029817930 scopus 로고    scopus 로고
    • Stonustoxin is a novel lethal factor from stonefish (Synanceja horrida) venom. cDNA cloning and characterisation
    • Ghadessy F.J., Chen D., Kini R.M., Chung M.C.M., Jeyaseelan K., Khoo H.E., Yuen R. Stonustoxin is a novel lethal factor from stonefish (Synanceja horrida) venom. cDNA cloning and characterisation. J. Biol. Chem. 271:1996;25575-25581.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25575-25581
    • Ghadessy, F.J.1    Chen, D.2    Kini, R.M.3    Chung, M.C.M.4    Jeyaseelan, K.5    Khoo, H.E.6    Yuen, R.7
  • 28
    • 0018845939 scopus 로고
    • Stopped-flow studies on the chemical modification with N-bromosuccinimide of model compounds of tryptophan residues
    • Ohnishi M., Kawagishi T., Abe T., Hiromi K. Stopped-flow studies on the chemical modification with N-bromosuccinimide of model compounds of tryptophan residues. J. Biochem. 87:1980;273-279.
    • (1980) J. Biochem. , vol.87 , pp. 273-279
    • Ohnishi, M.1    Kawagishi, T.2    Abe, T.3    Hiromi, K.4
  • 29
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein E.A., Vedenkina N.S., Ivkova M.N. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18:1973;263-279.
    • (1973) Photochem. Photobiol. , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 30
    • 0029086917 scopus 로고
    • Activation of chicken liver dihydrofolate reductase in concentrated urea solutions
    • Fan Y.X., Ju M., Zhou J., Tsou C. Activation of chicken liver dihydrofolate reductase in concentrated urea solutions. Biochim. Biophys. Acta. 1252:1995;151-157.
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 151-157
    • Fan, Y.X.1    Ju, M.2    Zhou, J.3    Tsou, C.4
  • 31
    • 0028589946 scopus 로고
    • Energy transfer from tryptophan residues of proteins to ANS
    • Chang L.S., Wen E.Y., Hung J.J., Chang C.C. Energy transfer from tryptophan residues of proteins to ANS. J. Prot. Chem. 13:1994;635-640.
    • (1994) J. Prot. Chem. , vol.13 , pp. 635-640
    • Chang, L.S.1    Wen, E.Y.2    Hung, J.J.3    Chang, C.C.4
  • 33
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink L.A. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:1995;495-522.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 495-522
    • Fink, L.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.