Isolation and characterization of a heparin with high anticoagulant activity from Anomalocardia brasiliana.
The isolation, some structural features, physicochemical properties and pharmacological activities of a heparin from Anomalocardia brasiliana are reported. It is shown that the mollusc heparin is very similar to those present in mammalian tissues with regard to chemical composition, physicochemical properties, pharmacological activities and susceptibility to heparinase and heparitinase II from Flavobacterium heparinum, as well as to the types of products formed by the action of these enzymes. Three significant quantitative differences were observed for the mollusc heparin when compared with the ones from mammalian origin, namely, a higher degree of binding with antithrombin III (45%), higher molecular weight (27-43 kDa) and higher anticoagulant activity (320 I.U./mg). The possible biological role of heparin is discussed in view of the present findings.
D000818:Animals; D000991:Antithrombins / Q000032:analysis; D001464:Barium; D001777:Blood Coagulation / Q000187:drug effects; D002417:Cattle; D011232:Chemical Precipitation; D006493:Heparin / Q000302:isolation & purification* / Q000494:pharmacology; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008974:Mollusca / Q000032:analysis*; D009608:Nitrous Acid; D011485:Protein Binding
D000991:Antithrombins; D001464:Barium; D006493:Heparin; D009608:Nitrous Acid