Purification and Characterization of a Plasminogen Activator Secreted by Cultured Human Pancreatic Carcinoma Cells

Wu Ming-chi, Grace K. Arimura, Adel A. Yunis

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Abstract

A plasminogen activator secreted by cultured human pancreatic carcinoma (Mia PaCa-2) cells has been purified to apparent homogeneity by procedures including Sepharose-l-arginine methyl ester affinity chromatography, Sephadex G-200 gel filtration, isoelectric focusing, and sodium dodecyl sulfate gel electrophoresis. The plasminogen activator shares many properties with urokinase including: molecular weight (55 000), isoelectric point (8.7), heat stability (60 °C, 30 min), pH stability (1.5–10), and its mode of activation of plasminogen. The intracellular enzyme is membrane bound and can be solubilized by detergent. Solubilized activator has a molecular weight similar to that of the secreted enzyme as determined by sodium dodecyl sulfate gel electrophoresis. The production of plasminogen activator by Mia PaCa-2 cells is totally inhibited by actinomycin D and cycloheximide.

Original languageEnglish (US)
Pages (from-to)1908-1913
Number of pages6
JournalBiochemistry
Volume16
Issue number9
DOIs
StatePublished - May 1 1977

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ASJC Scopus subject areas

  • Biochemistry

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