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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jbsc/016/04/0223-0233

    • Keywords

       

      Plasminogen activator; urokinase; fibrinolysis; Fibrin; lymphosarcoma

    • 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.

    • Author Affiliations

       

      M W Nulkar1 Rukmini Darad1 M Subramanian1 A R Pawse1

      1. Biochemistry Division, Bhabha Atomic Research Centre, Trombay, Bombay - 400 085, India
    • Dates

       
  • Journal of Biosciences | News

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