Purification and characterization of a cellular fibrinolytic factor associated with oncogenic transformation: The plasminogen activator from SV-40-transformed hamster cells

  • Judith K. Christman
  • , George Acs

Research output: Contribution to journalArticlepeer-review

98 Scopus citations

Abstract

Neoplastic cells, whether transformed by oncogenic viruses or chemical agents, release a fibrinolytic factor not released by normal cells. We have purified this factor 14 000-fold from the supernatant culture fluid of SV-40-transformed hamster cells. It is a plasminogen activator with a molecular weight of approx. 50 000 consisting of subunits linked by disulphide bridges. It is irreversibly inhibited by diisopropylfluorophosphate, indicating that it is a serine protease. The subunit contianing the diisopropylfluorophosphate binding site has a molecular weight of approx. 25 000.

Original languageEnglish
Pages (from-to)339-347
Number of pages9
JournalBBA Section Nucleic Acids And Protein Synthesis
Volume340
Issue number3
DOIs
StatePublished - 27 Mar 1974
Externally publishedYes

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