Nulkar, M WDarad, RukminiSubramanian, MPawse, A R2015-07-282015-07-281991-12Nulkar M W, Darad Rukmini, Subramanian M, Pawse A R. Plasminogen activator: Isolation and purification from lymphosarcoma of ascites bearing mice. Journal of Biosciences. 1991 Dec; 16(4): 223-233.http://imsear.searo.who.int/handle/123456789/160800Plasminogen 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.enPlasminogen activatorurokinasefibrinolysisFibrinlymphosarcomaArticle