title: Secretion of a proteolytic anticoagulant by Ancylostoma hookworms.
abstract: Hookworms of the genus Ancylostoma secrete an anticoagulant that both inhibits the clotting of human plasma and promotes fibrin clot dissolution. This anticoagulant activity is attributable to a 36,000 dalton proteolytic enzyme. The protease can degrade fibrinogen into five smaller polypeptides that intrinsically have anticoagulating properties, covert plasminogen to a mini-plasminogen-like molecule, and hydrolyze a synthetic peptide substrate with specificity for elastolytic enzymes. It is hypothesized that the parasite uses this enzyme to prevent blood clotting while feeding on villous capillaries.
mesh_terms: D000722:Ancylostoma / Q000201:enzymology*; D000724:Ancylostomiasis / Q000097:blood / Q000469:parasitology*; D000818:Animals; D001777:Blood Coagulation; D004285:Dogs; D004547:Elastic Tissue / Q000378:metabolism; D005338:Fibrin Fibrinogen Degradation Products / Q000032:analysis; D005342:Fibrinolysis; D006801:Humans; D008970:Molecular Weight; D010314:Partial Thromboplastin Time; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism* / Q000502:physiology; D011517:Prothrombin Time
chemical_list: D005338:Fibrin Fibrinogen Degradation Products; D010447:Peptide Hydrolases