The anticoagulant action of phospholipase A from Eresus niger spider venom.
Phospholipase A, named component EnPA, was isolated from Eresus niger spider venom. It was determined to be a single peptide chain with mol. wt of 13,000. Component EnPA showed high anticoagulant activity when the APTT was measured in spite of its low enzymatic activity (30 +/- 6 mumol/min/mg). It was concluded that anticoagulant action of compound EnPA is due to inactivation of the procoagulant activity of phospholipids because of its high binding with them.
Usmanov
P B
PB
Institute of Physiology and Biophysics, Uzbek Academy of Sciences, Tashkent.
Nuritova
F A
FA
D001777:Blood Coagulation / Q000187:drug effects*; D006801:Humans; D010741:Phospholipases A / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D013045:Species Specificity; D013111:Spider Venoms / Q000737:chemistry*
D013111:Spider Venoms; D010741:Phospholipases A