title: Contact activation of plasma: structure-activity relationships of human high molecular weight kininogen.
abstract: Human high MW kininogen can be isolated as a single polypeptide chain of 110,000 MW. Purified human plasma kallikrein cleaves this molecule to give a disulfide-linked, two chain molecule, free of kinin, that retains full clotting activity. Following reduction and carboxymethylation of the two chain molecule, a light chain can be isolated that quantitatively retains the full coagulant activity of the native molecule. During contact activation in normal human plasma a rapid cleavage of high MW kininogen along with kinin liberation occurs in a reaction that is dependent upon the presence of prekallikrein and Factor XII (Hageman factor).
mesh_terms: D001777:Blood Coagulation; D006801:Humans; D007700:Kinetics; D007704:Kininogens / Q000097:blood*; D007705:Kinins / Q000097:blood; D046911:Macromolecular Substances; D008970:Molecular Weight; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D007704:Kininogens; D007705:Kinins; D046911:Macromolecular Substances