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Immobilization of plasminogen on Escherichia coli flagella

Kaarina Lähteenmäki , Benita Westerlund , Pentti Kuusela , Timo K. Korhonen
DOI: http://dx.doi.org/10.1111/j.1574-6968.1993.tb05981.x 309-314 First published online: 1 February 1993

Abstract

The interaction of plasminogen with flagella of Escherichia coli was investigated. Plasminogen bound to flagella purified from E. coli LE392, a commonly used cloning host, and E. coli IH3069, and O25H1 strain isolated from a case of newborn bacteremia. The binding was inhibited by the lysine analog є-aminocaproic acid, suggesting involvement of the lysine-binding Kringle domains of plasminogen in the binding. Purified flagella enhanced the formation of plasmin activity in the presence of tissue-type plasminogen activator; a similar enhancement was observed with flagella-expressing LE392 cells.

Key words
  • Escherichia coli
  • Flagella
  • Plasminogen
  • Proteolysis

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