Venom from spiders of the genus Hippasa: biochemical and pharmacological studies.
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 PLA2 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.
Nagaraju
S
S
Department of Biochemistry, University of Mysore, Manasagangotri, Mysore, India.
Mahadeswaraswamy
Y H
YH
Girish
K S
KS
Kemparaju
K
K
D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects; D002286:Carcinoma, Ehrlich Tumor; D002470:Cell Survival / Q000187:drug effects; D003402:Creatine Kinase / Q000097:blood; D004487:Edema / Q000139:chemically induced; D005260:Female; D005340:Fibrinogen / Q000378:metabolism; D006470:Hemorrhage / Q000139:chemically induced; D006801:Humans; D006821:Hyaluronoglucosaminidase / Q000378:metabolism; D007770:L-Lactate Dehydrogenase / Q000097:blood; D051379:Mice; D018482:Muscle, Skeletal / Q000187:drug effects / Q000502:physiology; D010741:Phospholipases A / Q000378:metabolism; D054467:Phospholipases A2; D011506:Proteins / Q000032:analysis; D011898:Ranidae; D012867:Skin / Q000187:drug effects / Q000473:pathology; D013111:Spider Venoms / Q000737:chemistry* / Q000494:pharmacology*; D013112:Spiders; D014407:Tumor Cells, Cultured
D011506:Proteins; D013111:Spider Venoms; D005340:Fibrinogen; D007770:L-Lactate Dehydrogenase; D003402:Creatine Kinase; D010741:Phospholipases A; D054467:Phospholipases A2; D006821:Hyaluronoglucosaminidase