Plasminogen activator: Isolation and purification from lymphosarcoma of ascites bearing mice.
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Date
1991-12
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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.
Description
Keywords
Plasminogen activator, urokinase, fibrinolysis, Fibrin, lymphosarcoma
Citation
Nulkar 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.