Purification and characterization of a plasminogen activator secreted by cultured human pancreatic carcinoma cells

Ming C. Wu, 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
StatePublished - 1977

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Plasminogen Activators
Purification
Gels
Cells
Electrophoresis
Sodium Dodecyl Sulfate
Molecular Weight
Molecular weight
Affinity chromatography
Plasminogen
Urokinase-Type Plasminogen Activator
Isoelectric Point
Isoelectric Focusing
Dactinomycin
Enzymes
Cycloheximide
Affinity Chromatography
Detergents
Sepharose
Gel Chromatography

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purification and characterization of a plasminogen activator secreted by cultured human pancreatic carcinoma cells. / Wu, Ming C.; Arimura, Grace K.; Yunis, Adel A.

In: Biochemistry, Vol. 16, No. 9, 1977, p. 1908-1913.

Research output: Contribution to journalArticle

Wu, Ming C. ; Arimura, Grace K. ; Yunis, Adel A. / Purification and characterization of a plasminogen activator secreted by cultured human pancreatic carcinoma cells. In: Biochemistry. 1977 ; Vol. 16, No. 9. pp. 1908-1913.
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