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Volumn 78, Issue 13, 2006, Pages 1433-1440

Inhibition of Naja naja venom hyaluronidase: Role in the management of poisonous bite

Author keywords

Aristolochic acid; Cobra (Naja naja) venom; Hyaluronidase; Venom neutralization

Indexed keywords

SNAKE VENOM;

EID: 32544431758     PISSN: 00243205     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lfs.2005.07.015     Document Type: Article
Times cited : (60)

References (29)
  • 1
    • 0036027944 scopus 로고    scopus 로고
    • Neutralization of a snake venom haemorrhagic metalloproteinase prevents coagulopathy after subcutaneous injection of Bothrops jararaca venom in rats
    • K. Anai, M. Sugiki, E. Yoshida, and M. Maruyama Neutralization of a snake venom haemorrhagic metalloproteinase prevents coagulopathy after subcutaneous injection of Bothrops jararaca venom in rats Toxicon 40 2002 63 68
    • (2002) Toxicon , Issue.40 , pp. 63-68
    • Anai, K.1    Sugiki, M.2    Yoshida, E.3    Maruyama, M.4
  • 2
    • 0025931518 scopus 로고
    • Snake venom variability: Methods of study results and interpretations
    • J.P. Chippaux, J. Williams, and White Snake venom variability: methods of study results and interpretations Toxicon 29 1991 1279 1303
    • (1991) Toxicon , Issue.29 , pp. 1279-1303
    • Chippaux, J.P.1    Williams, J.2    White3
  • 4
    • 2342462926 scopus 로고    scopus 로고
    • Isolation and characterization of hyaluronidase a "spreading factor" from Indian cobra (Naja naja) venom
    • K.S. Girish, R. Shashidhara murthy, S. Nagaraju, T.V. Gowda, and K. Kemparaju Isolation and characterization of hyaluronidase a "spreading factor" from Indian cobra (Naja naja) venom Biochimie 86 2004 193 202
    • (2004) Biochimie , Issue.86 , pp. 193-202
    • Girish, K.S.1    Shashidhara Murthy, R.2    Nagaraju, S.3    Gowda, T.V.4    Kemparaju, K.5
  • 6
    • 0023876101 scopus 로고
    • An alternative in vitro method for testing the potency of the polyvalent antivenom produced in Costa Rica
    • J.M. Gutierrez, C. Avila, G. Rojas, and L. Cerdas An alternative in vitro method for testing the potency of the polyvalent antivenom produced in Costa Rica Toxicon 26 1988 411 413
    • (1988) Toxicon , Issue.26 , pp. 411-413
    • Gutierrez, J.M.1    Avila, C.2    Rojas, G.3    Cerdas, L.4
  • 7
    • 0025209888 scopus 로고
    • Changes in myofibrillar components after skeletal muscle necrosis induced by a myotoxin isolated from the venom of the snake Bothrops asper
    • J.M. Gutierrez, V. Arce, F. Brenes, and F. Chaves Changes in myofibrillar components after skeletal muscle necrosis induced by a myotoxin isolated from the venom of the snake Bothrops asper Experimental and Molecular Pathology 52 1990 25 36
    • (1990) Experimental and Molecular Pathology , Issue.52 , pp. 25-36
    • Gutierrez, J.M.1    Arce, V.2    Brenes, F.3    Chaves, F.4
  • 8
    • 0001798502 scopus 로고
    • Immunoblotting
    • C.S.H. Laboratory Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • E. Harlow, and D. Lane Immunoblotting C.S.H. Laboratory Antibodies: A Laboratory Manual 1988 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 471 510
    • (1988) Antibodies: A Laboratory Manual , pp. 471-510
    • Harlow, E.1    Lane, D.2
  • 9
    • 0343363079 scopus 로고
    • Preparation of γ-globulin
    • D.M. Weir Academic Press New York
    • K. Heide, and H.G. Schwick Preparation of γ-globulin D.M. Weir Handbook of Experimental Immunology vol. 1 1973 Academic Press New York 61
    • (1973) Handbook of Experimental Immunology , vol.1 , pp. 61
    • Heide, K.1    Schwick, H.G.2
  • 10
    • 0024536883 scopus 로고
    • 2 from Russell's viper (Vipera russelii) venom
    • 2 from Russell's viper (Vipera russelii) venom Toxicon 27 1989 229 237
    • (1989) Toxicon , Issue.27 , pp. 229-237
    • Kasturi, S.1    Gowda, T.V.2
  • 12
    • 0031740746 scopus 로고    scopus 로고
    • Proline brackets and identification of potential functional sites in proteins: Toxins to therapeutics
    • R.M. Kini Proline brackets and identification of potential functional sites in proteins: toxins to therapeutics Toxicon 36 1998 1659 1670
    • (1998) Toxicon , Issue.36 , pp. 1659-1670
    • Kini, R.M.1
  • 14
    • 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 , Issue.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 19244367926 scopus 로고    scopus 로고
    • Comparative study on the ability of IgG and Fab sheep antivenoms to neutralize local hemorrhage, edema and myonecrosis induced by Bothrops asper (terciopelo) snake venom
    • G. Leon, J.M. Valverde, G. Rojas, B. Lomonte, and J.M. Gutierrez Comparative study on the ability of IgG and Fab sheep antivenoms to neutralize local hemorrhage, edema and myonecrosis induced by Bothrops asper (terciopelo) snake venom Toxicon 38 2000 233 244
    • (2000) Toxicon , Issue.38 , pp. 233-244
    • Leon, G.1    Valverde, J.M.2    Rojas, G.3    Lomonte, B.4    Gutierrez, J.M.5
  • 16
    • 0030273220 scopus 로고    scopus 로고
    • Similar effectiveness of Fab and F(ab′)2 antivenoms in neutralization of hemorrhagic activity of Vipera berus snake venom in mice
    • B. Lomonte, G. Leon, and L.A. Hanson Similar effectiveness of Fab and F(ab′)2 antivenoms in neutralization of hemorrhagic activity of Vipera berus snake venom in mice Toxicon 34 1996 1197 1202
    • (1996) Toxicon , Issue.34 , pp. 1197-1202
    • Lomonte, B.1    Leon, G.2    Hanson, L.A.3
  • 18
    • 0034862658 scopus 로고    scopus 로고
    • Clostridial hydrolytic enzymes degrading extracellular components
    • O. Matsushita, and A. Okabe Clostridial hydrolytic enzymes degrading extracellular components Toxicon 39 2001 1769 1780
    • (2001) Toxicon , Issue.39 , pp. 1769-1780
    • Matsushita, O.1    Okabe, A.2
  • 19
    • 0022556249 scopus 로고
    • 50 determination of snake venoms using eight to ten experimental animals
    • 50 determination of snake venoms using eight to ten experimental animals Toxicon 24 1986 395 401
    • (1986) Toxicon , Issue.24 , pp. 395-401
    • Meier, J.1    Theakston, R.D.G.2
  • 21
    • 0024441845 scopus 로고
    • Immunological relationships of phospholipase A2 neurotoxins from snake venoms
    • J.L. Middlebrook, and I.I. Kaiser Immunological relationships of phospholipase A2 neurotoxins from snake venoms Toxicon 27 1989 965 977
    • (1989) Toxicon , Issue.27 , pp. 965-977
    • Middlebrook, J.L.1    Kaiser, I.I.2
  • 22
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugars
    • J.L. Reissig, J.L. Stominger, and L.F. Leloir A modified colorimetric method for the estimation of N-acetylamino sugars Journal of Biological Chemistry 217 1955 959 969
    • (1955) Journal of Biological Chemistry , Issue.217 , pp. 959-969
    • Reissig, J.L.1    Stominger, J.L.2    Leloir, L.F.3
  • 24
    • 0032919106 scopus 로고    scopus 로고
    • Diet and snake venom variation: Can local selection alone explain intraspecific venom variation?
    • M. Sasa Diet and snake venom variation: can local selection alone explain intraspecific venom variation? Toxicon 37 1999 249 252
    • (1999) Toxicon , Issue.37 , pp. 249-252
    • Sasa, M.1
  • 25
    • 0026719419 scopus 로고
    • An ELISA-like assay for hyaluronidase and hyaluronidase inhibitors
    • M. Stern, and R. Stern An ELISA-like assay for hyaluronidase and hyaluronidase inhibitors Matrix 12 1992 397 403
    • (1992) Matrix , Issue.12 , pp. 397-403
    • Stern, M.1    Stern, R.2
  • 26
    • 0021001085 scopus 로고
    • Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor
    • A.T. Tu, and R.R. Hendon Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor Comparative Biochemistry and Physiology 76B 1983 337 383
    • (1983) Comparative Biochemistry and Physiology , Issue.76 B , pp. 337-383
    • Tu, A.T.1    Hendon, R.R.2
  • 29
    • 0242352551 scopus 로고    scopus 로고
    • Hyaluronidase inhibitors (sodium cromoglycate and sodium auro-thiomalate) reduce the local tissue damage and prolong the survival time of mice injected with Naja kaouthia and Calloselasma rhodostoma venoms
    • S. Yingprasertchai, S. Bunyasrisawt, and K. Ratanabanangkoon Hyaluronidase inhibitors (sodium cromoglycate and sodium auro-thiomalate) reduce the local tissue damage and prolong the survival time of mice injected with Naja kaouthia and Calloselasma rhodostoma venoms Toxicon 42 2003 635 646
    • (2003) Toxicon , Issue.42 , pp. 635-646
    • Yingprasertchai, S.1    Bunyasrisawt, S.2    Ratanabanangkoon, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.