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Venom from spiders of the genusHippasa: Biochemical and pharmacological studies

Authors
Journal
Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology
1532-0456
Publisher
Elsevier
Publication Date
Volume
144
Issue
1
Identifiers
DOI: 10.1016/j.cbpc.2006.04.016
Keywords
  • Spider Venom
  • Venom Variability
  • H. Partita
  • H. Agelenoides
  • H. Lycosina
  • Phospholipase A2
  • Fibrinogenolysis
  • Hemorrhage
  • Myotoxicity
  • Neurotoxicity
Disciplines
  • Biology
  • Chemistry
  • Medicine
  • Pharmacology

Abstract

Abstract The venoms from female spiders of the genus Hippasa namely H. partita, H. agelenoides and H. lycosina are compared for biochemical and pharmacological properties. SDS-PAGE pattern revealed varied protein composition. Marked variability is seen with casein hydrolyzing enzymes in SDS-PAGE zymogram. H. partita venom was the only venom that hydrolyzed gelatin while the other two venoms did not. The venoms shared similar hyaluronidase activity, showing a single activity band in SDS-PAGE zymogram. The PLA 2 activity varied as H. partita > H. agelenoides > H. lycosina venoms. Marked differences were noted in the ability to induce edema, cytotoxicity, myotoxicity and neurotoxicity, while hemorrhage was associated exclusively with H. partita venom.

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