title: Partial purification and characterization of native plasminogen activators from bovine milk.
abstract: At least four native plasminogen activators were detected in bovine milk, and two partially purified plasminogen activators were characterized. The plasminogen activators were dissociated from casein proteins by treatments with sulfuric acid and dimethylformamide. The plasminogen activators in the resulting fractions were partially purified with size exclusion, affinity, or metal chelate chromatographic techniques. Molecular weights of the two partially purified plasminogen activators were 47.2 and 30.5 kDa by gel electrophoresis. Size exclusion chromatography gave a molecular weight of 43.2 kDa for the first plasminogen activator. The isoelectric points of the two plasminogen activators were in the pH range 6.2 to 6.7. Because activity was not enhanced by the presence of fibrinogen fragments in a plasminogen activator assay mixture and decreased when human anti-urokinase Ig were added, at least some bovine milk native plasminogen activators appear to be urokinase-type plasminogen activators.
authors.affiliation: Department of Food Science, Purdue University, West Lafayette, IN 47907.
authors.forename: G
authors.initials: G
authors.lastname: Deharveng
authors.forename: S S
authors.initials: SS
authors.lastname: Nielsen
mesh_terms: D000818:Animals; D002417:Cattle; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D008892:Milk / Q000201:enzymology*; D008970:Molecular Weight; D010960:Plasminogen Activators / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D010960:Plasminogen Activators