Plasminogen activator: Isolation and purification from lymphosarcoma of ascites bearing mice.

dc.contributor.authorNulkar, M W
dc.contributor.authorDarad, Rukmini
dc.contributor.authorSubramanian, M
dc.contributor.authorPawse, A R
dc.date.accessioned2015-07-28T11:22:18Z
dc.date.available2015-07-28T11:22:18Z
dc.date.issued1991-12
dc.description.abstractPlasminogen 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.en_US
dc.identifier.citationNulkar 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.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/160800
dc.language.isoenen_US
dc.source.urihttps://www.ias.ac.in/jarch/jbiosci/16/223-233.pdfen_US
dc.subjectPlasminogen activatoren_US
dc.subjecturokinaseen_US
dc.subjectfibrinolysisen_US
dc.subjectFibrinen_US
dc.subjectlymphosarcomaen_US
dc.titlePlasminogen activator: Isolation and purification from lymphosarcoma of ascites bearing mice.en_US
dc.typeArticleen_US
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