Plasminogen activator: Isolation and purification from Lymphosarcoma of ascites bearing mice |
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Authors: | M. W. Nulkar Rukmini Darad M. Subramanian A. R. Pawse |
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Affiliation: | (1) Biochemistry Division, Bhabha Atomic Research Centre, Trombay, 400 085 Bombay, India |
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Abstract: | Plasminogen activator secreted by lymphosarcoma (ascites) of mice was purified up to 163-fold by ammonium sulphate fractionation at 35% saturation and chromatography on p-aminobenzamidine-Sepharose 4B. The purified activator contained specific activity of 9980 IU/mg. The plasminogen activator displayed homogeneity by polyacrylamide slab gel electrophoresis and high performance liquid chromatography. The activator consisted of a single polypeptide chain with an apparent molecular weight of 66,000 daltons as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis under reducing conditions as well as gel filtration on Sephadex G-100. Distinct differences between this activator and urokinase were discernible in respect of specific activities, fibrin affinity and immunochemical properties. The lymphosarcoma activator appears to be of tissue-type origin since it showed gross similarity to standard tissue plasminogen activator in terms of modes of binding to fibrin and immunological attributes. |
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Keywords: | Plasminogen activator urokinase fibrinolysis Fibrin lymphosarcoma |
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