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A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system BJMBR
Yarzábal,A.; Avilán,L.; Hoelzl,K.; Muñoz,M. de; Puig,J.; Kansau,I..
The interaction of plasminogen, tissue plasminogen activator (t-PA) and urokinase with a clinical strain of Helicobacter pylori was studied. Plasminogen bound to the surface of H. pylori cells in a concentration-dependent manner and could be activated to the enzymatic form, plasmin, by t-PA. Affinity chromatography assays revealed a plasminogen-binding protein of 58.9 kDa in water extracts of surface proteins. Surface-associated plasmin activity, detected with the chromogenic substrate CBS 00.65, was observed only when plasminogen and an exogenous activator were added to the cell suspension. The two physiologic plasminogen activators, t-PA and urokinase, were also shown to bind to and remain active on the surface of bacterial cells. epsilon-Aminocaproic...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Helicobacter pylori; Plasminogen; T-PA; Urokinase; Plasminogen activation.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000900004
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