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Volumn 50, Issue 3, 2007, Pages 383-393

Purification and properties of hyaluronidase from Hippasa partita (funnel web spider) venom gland extract

Author keywords

Hippasa partita venom gland extract.; Hyaluronic acid; Hyaluronidase; Spreading factor

Indexed keywords

ANTISERUM; CATION; CHLORIDE ION; DIVALENT CATION; HEMORRHAGIC METALLOPROTEASE COMPLEX I; HYALURONIC ACID; HYALURONIDASE; METALLOPROTEINASE; POTASSIUM ION; PRECIPITIN; SEPHADEX; SODIUM CHLORIDE; SODIUM ION; SPIDER VENOM; UNCLASSIFIED DRUG;

EID: 34447649568     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2007.04.007     Document Type: Article
Times cited : (43)

References (41)
  • 1
    • 0024452930 scopus 로고
    • Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases
    • Baramova E.N., Shannon J.D., Bjarnason J.B., and Fox J.W. Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases. Arch. Biochem. Biophys. 275 (1989) 63-71
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 63-71
    • Baramova, E.N.1    Shannon, J.D.2    Bjarnason, J.B.3    Fox, J.W.4
  • 2
    • 13944265640 scopus 로고    scopus 로고
    • Enzymatic characterizations, antigenic cross reactivity and neutralization of dermonecrotic activity of five Loxosceles spider venoms of medical importance in the Americas
    • Barbaro K.C., Knysak I., Martins R., Hogan C., and Winkel K. Enzymatic characterizations, antigenic cross reactivity and neutralization of dermonecrotic activity of five Loxosceles spider venoms of medical importance in the Americas. Toxicon 45 (2005) 489-499
    • (2005) Toxicon , vol.45 , pp. 489-499
    • Barbaro, K.C.1    Knysak, I.2    Martins, R.3    Hogan, C.4    Winkel, K.5
  • 3
    • 0026663986 scopus 로고
    • Molecular mass determination and assay of venom hyaluronidases by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Cevallos M.A., Navarro-Duque C., Varela-Julia M., and Alagon A.C. Molecular mass determination and assay of venom hyaluronidases by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Toxicon 30 (1992) 925-930
    • (1992) Toxicon , vol.30 , pp. 925-930
    • Cevallos, M.A.1    Navarro-Duque, C.2    Varela-Julia, M.3    Alagon, A.C.4
  • 6
    • 34247094744 scopus 로고    scopus 로고
    • Hyaluronidases in Loxosceles intermedia (Brown spider) venom are endo- β-N-acetyl- d- hexosaminidases hydrolases
    • da Silveira R.B., Chaim O.M., Mangili O.C., Gremski W., Dietrich C.P., Nader H.B., and Veiga S.S. Hyaluronidases in Loxosceles intermedia (Brown spider) venom are endo- β-N-acetyl- d- hexosaminidases hydrolases. Toxicon 49 6 (2007) 758-768
    • (2007) Toxicon , vol.49 , Issue.6 , pp. 758-768
    • da Silveira, R.B.1    Chaim, O.M.2    Mangili, O.C.3    Gremski, W.4    Dietrich, C.P.5    Nader, H.B.6    Veiga, S.S.7
  • 7
    • 0001615705 scopus 로고
    • Turbidimetric measurement of acid mucopolysaccharides and hyaluronidase activity
    • Ferrente N.D. Turbidimetric measurement of acid mucopolysaccharides and hyaluronidase activity. J. Biol. Chem. 220 (1956) 303-306
    • (1956) J. Biol. Chem. , vol.220 , pp. 303-306
    • Ferrente, N.D.1
  • 8
    • 0030343997 scopus 로고    scopus 로고
    • The hyaluronidase; a chemical biological and clinical overview
    • Frost G.I., Csoka T., and Stern R. The hyaluronidase; a chemical biological and clinical overview. Trends Glycosc. Glycotechnol. 8 (1996) 419-434
    • (1996) Trends Glycosc. Glycotechnol. , vol.8 , pp. 419-434
    • Frost, G.I.1    Csoka, T.2    Stern, R.3
  • 9
    • 32544431758 scopus 로고    scopus 로고
    • Inhibition of Naja naja venom hyaluronidase: role in the management of poisonous bite
    • Girish K.S., and Kemparaju K. Inhibition of Naja naja venom hyaluronidase: role in the management of poisonous bite. Life Sci. 78 13 (2006) 1433-1440
    • (2006) Life Sci. , vol.78 , Issue.13 , pp. 1433-1440
    • Girish, K.S.1    Kemparaju, K.2
  • 10
    • 0036854659 scopus 로고    scopus 로고
    • Snake venom hyaluronidase: an evidence for isoforms and extracellular matrix degradation
    • Girish K.S., Jagadeesha D.K., Rajeev K.B., and Kemparaju K. Snake venom hyaluronidase: an evidence for isoforms and extracellular matrix degradation. Mol. Cell. Biochem. 240 (2002) 105-110
    • (2002) Mol. Cell. Biochem. , vol.240 , pp. 105-110
    • Girish, K.S.1    Jagadeesha, D.K.2    Rajeev, K.B.3    Kemparaju, K.4
  • 11
    • 2342462926 scopus 로고    scopus 로고
    • Isolation and characterization of hyaluronidase a 'spreading factor' from Indian cobra (Naja naja) venom
    • Girish K.S., Shashidharamurthy R., Nagaraju S., Gowda T.V., and Kemparaju K. Isolation and characterization of hyaluronidase a 'spreading factor' from Indian cobra (Naja naja) venom. Biochimie 86 (2004) 193-202
    • (2004) Biochimie , vol.86 , pp. 193-202
    • Girish, K.S.1    Shashidharamurthy, R.2    Nagaraju, S.3    Gowda, T.V.4    Kemparaju, K.5
  • 12
    • 0025209888 scopus 로고
    • Changes in myofibrillar components after skeletal muscle necrosis induced by a myotoxin isolated from the venom of the snake Bothrops asper
    • Gutierrez J.M., Arce V., Brenes F., and Chaves F. Changes in myofibrillar components after skeletal muscle necrosis induced by a myotoxin isolated from the venom of the snake Bothrops asper. Exp. Mol. Pathol. 52 (1990) 25-37
    • (1990) Exp. Mol. Pathol. , vol.52 , pp. 25-37
    • Gutierrez, J.M.1    Arce, V.2    Brenes, F.3    Chaves, F.4
  • 13
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imato T., and Yagishitha K. A simple activity measurement of lysozyme. Agric. Biol. Chem. 33 (1971) 1154-1157
    • (1971) Agric. Biol. Chem. , vol.33 , pp. 1154-1157
    • Imato, T.1    Yagishitha, K.2
  • 14
    • 0002797372 scopus 로고
    • Enzymatic activity of spider venoms
    • Buckley E.E., and Porges N. (Eds), Ameriacan Association for the Advancement of Science, Washington, DC
    • Kaiser E. Enzymatic activity of spider venoms. In: Buckley E.E., and Porges N. (Eds). Venoms (1956), Ameriacan Association for the Advancement of Science, Washington, DC 91-93
    • (1956) Venoms , pp. 91-93
    • Kaiser, E.1
  • 15
    • 0024536883 scopus 로고
    • Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelii) venom
    • Kasturi S., and Gowda T.V. Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelii) venom. Toxicon 27 (1988) 229-237
    • (1988) Toxicon , vol.27 , pp. 229-237
    • Kasturi, S.1    Gowda, T.V.2
  • 16
    • 0021343667 scopus 로고
    • The purification and characterization of hyaluronidase from the venom of the honey bee, Apis mellifera
    • Kemeny D.M., Dalton N., Lowrence A.J., Pearce F.L., and Vernon C.A. The purification and characterization of hyaluronidase from the venom of the honey bee, Apis mellifera. Eur. J. Biochem. 139 (1984) 217-223
    • (1984) Eur. J. Biochem. , vol.139 , pp. 217-223
    • Kemeny, D.M.1    Dalton, N.2    Lowrence, A.J.3    Pearce, F.L.4    Vernon, C.A.5
  • 17
    • 84961047247 scopus 로고
    • A studies on the quantitative method from determination of haemorrhagic activity of Habu snake venom
    • Kondo H., Kondo S., Itezawa H., Murata R., and Ohasaka A. A studies on the quantitative method from determination of haemorrhagic activity of Habu snake venom. Jpn. J. Med. Sci. Biol. 13 (1969) 43-51
    • (1969) Jpn. J. Med. Sci. Biol. , vol.13 , pp. 43-51
    • Kondo, H.1    Kondo, S.2    Itezawa, H.3    Murata, R.4    Ohasaka, A.5
  • 18
    • 0029079957 scopus 로고
    • Hyaluronidases-a group of neglected enzymes
    • Kreil G. Hyaluronidases-a group of neglected enzymes. Protein Sci. 4 (1995) 1666-1669
    • (1995) Protein Sci. , vol.4 , pp. 1666-1669
    • Kreil, G.1
  • 19
    • 0035864381 scopus 로고    scopus 로고
    • Characterization of hyaluronidase isolated from Agkistrodon contortrix contortrix (Southern copperhead) venom
    • Kudo K., and Tu A.T. Characterization of hyaluronidase isolated from Agkistrodon contortrix contortrix (Southern copperhead) venom. Arch. Biochem. Biophys. 386 (2001) 154-162
    • (2001) Arch. Biochem. Biophys. , vol.386 , pp. 154-162
    • Kudo, K.1    Tu, A.T.2
  • 20
    • 0028218809 scopus 로고
    • Purification of toxic peptides and the aminoacid sequence of CSTX-1 from the multicomponent venom of Cupiennius salei (Araneae: ctenidae)
    • Kuhn-Nentwig L., Schaller J., and Nentwig W. Purification of toxic peptides and the aminoacid sequence of CSTX-1 from the multicomponent venom of Cupiennius salei (Araneae: ctenidae). Toxicon 32 (1994) 287-302
    • (1994) Toxicon , vol.32 , pp. 287-302
    • Kuhn-Nentwig, L.1    Schaller, J.2    Nentwig, W.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 25
    • 0026480614 scopus 로고
    • Broad substrate specificity of snake venom fibrinolytic enzymes: possible role in hemorrhage
    • Maruyama M., Sugiki M., Yoshida E., Shimaya K., and Mihara H. Broad substrate specificity of snake venom fibrinolytic enzymes: possible role in hemorrhage. Toxicon 30 (1992) 1387-1397
    • (1992) Toxicon , vol.30 , pp. 1387-1397
    • Maruyama, M.1    Sugiki, M.2    Yoshida, E.3    Shimaya, K.4    Mihara, H.5
  • 26
    • 0032508626 scopus 로고    scopus 로고
    • Hyaluronidase and its substrate hyaluronan: biochemistry, biological activities and therapeutic uses
    • Menzel E.J., and Farr C. Hyaluronidase and its substrate hyaluronan: biochemistry, biological activities and therapeutic uses. Cancer Lett. 131 (1998) 3-11
    • (1998) Cancer Lett. , vol.131 , pp. 3-11
    • Menzel, E.J.1    Farr, C.2
  • 27
    • 77956924584 scopus 로고
    • Hyaluronidases
    • Boyer P.D. (Ed), Academic press, New York
    • Meyer K. Hyaluronidases. In: Boyer P.D. (Ed). In the Enzymes. 3rd ed. vol. V. (1971), Academic press, New York 307-320
    • (1971) In the Enzymes. 3rd ed. , vol.V , pp. 307-320
    • Meyer, K.1
  • 28
    • 0026069146 scopus 로고
    • Preparation and characterization of monoclonal antibodies against Pseudexin
    • Middlebrook J.L. Preparation and characterization of monoclonal antibodies against Pseudexin. Toxicon 29 (1991) 359-370
    • (1991) Toxicon , vol.29 , pp. 359-370
    • Middlebrook, J.L.1
  • 30
    • 0026541165 scopus 로고
    • Purification and partial characterization of hyaluronidase from stone fish (Synanceja horrida) venom
    • Poh C.H., Yeun R., Chung M.C., and Khoo H.E. Purification and partial characterization of hyaluronidase from stone fish (Synanceja horrida) venom. Comp. Biochem. Physol. 101B (1992) 159-163
    • (1992) Comp. Biochem. Physol. , vol.101 B , pp. 159-163
    • Poh, C.H.1    Yeun, R.2    Chung, M.C.3    Khoo, H.E.4
  • 31
    • 0025098399 scopus 로고
    • Isolation and characterization of hyaluronidase from scorpion (Heterometrus fulvipes) venom
    • Ramanaiah M., Parthasarathy P.R., and Venkaiah B. Isolation and characterization of hyaluronidase from scorpion (Heterometrus fulvipes) venom. Biochem. Int. 20 (1990) 301-310
    • (1990) Biochem. Int. , vol.20 , pp. 301-310
    • Ramanaiah, M.1    Parthasarathy, P.R.2    Venkaiah, B.3
  • 32
    • 0034768977 scopus 로고    scopus 로고
    • Pharmacology and biochemistry of spider venoms
    • Rash L.D., and Hodgson W.C. Pharmacology and biochemistry of spider venoms. Toxicon 40 (2002) 225-254
    • (2002) Toxicon , vol.40 , pp. 225-254
    • Rash, L.D.1    Hodgson, W.C.2
  • 33
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugars
    • Reissig J.L., Strominger J.L., and Leolir L.F. A modified colorimetric method for the estimation of N-acetylamino sugars. J. Biol. Chem. 217 (1955) 959-966
    • (1955) J. Biol. Chem. , vol.217 , pp. 959-966
    • Reissig, J.L.1    Strominger, J.L.2    Leolir, L.F.3
  • 35
    • 0021001085 scopus 로고
    • Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor
    • Tu A.T., and Hendon R.R. Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor. Comp. Biochem. Physiol. 76B (1983) 337-383
    • (1983) Comp. Biochem. Physiol. , vol.76 B , pp. 337-383
    • Tu, A.T.1    Hendon, R.R.2
  • 36
    • 34447620522 scopus 로고    scopus 로고
    • Uma, B., 1999. Comparative characterization of Hemorrhagins of Russell's viper (Vipera russelii) venom from different regions of India. Ph.D. Thesis, University of Mysore, Mysore, India, submitted.
  • 37
    • 0023186213 scopus 로고
    • Characterization of three edema inducing phospholipase A2 enzymes from habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristolochic acid
    • Vishwanath B.S., Kini R.M., and Gowda T.V. Characterization of three edema inducing phospholipase A2 enzymes from habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristolochic acid. Toxicon 25 (1987) 501-515
    • (1987) Toxicon , vol.25 , pp. 501-515
    • Vishwanath, B.S.1    Kini, R.M.2    Gowda, T.V.3
  • 39
    • 0015805632 scopus 로고
    • Hyaluronidase and esterase activities of the venom of poisonous brown recluse spider
    • Wright R.P., Elgert K.D., Campell B.J., and Barrett J.T. Hyaluronidase and esterase activities of the venom of poisonous brown recluse spider. Arch. Biochem. Biophys. 159 (1973) 415-426
    • (1973) Arch. Biochem. Biophys. , vol.159 , pp. 415-426
    • Wright, R.P.1    Elgert, K.D.2    Campell, B.J.3    Barrett, J.T.4
  • 40
    • 0020397002 scopus 로고
    • Purification and partial characterization of hyaluronidase from five pace snake (Agkistrodon acutus) venom
    • Xu X., Wang X., Xi X., Liu J., Huang J., and Lu Z. Purification and partial characterization of hyaluronidase from five pace snake (Agkistrodon acutus) venom. Toxicon 20 (1982) 973-981
    • (1982) Toxicon , vol.20 , pp. 973-981
    • Xu, X.1    Wang, X.2    Xi, X.3    Liu, J.4    Huang, J.5    Lu, Z.6
  • 41
    • 0034598661 scopus 로고    scopus 로고
    • Comparison of enzymatic activity from three species of necrotizing arachnids in Australia: Loxosceles rufescens, Badumma insignis and Lampona cylindrata
    • Young A.R., and Pincus S.J. Comparison of enzymatic activity from three species of necrotizing arachnids in Australia: Loxosceles rufescens, Badumma insignis and Lampona cylindrata. Toxicon 39 (2001) 391-400
    • (2001) Toxicon , vol.39 , pp. 391-400
    • Young, A.R.1    Pincus, S.J.2


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