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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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Cloning, expression and purification of recombinant streptokinase: partial characterization of the protein expressed in Escherichia coli BJMBR
Avilán,L.; Yarzábal,A.; Jürgensen,C.; Bastidas,M.; Cruz,J.; Puig,J..
We cloned the streptokinase (STK) gene of Streptococcus equisimilis in an expression vector of Escherichia coli to overexpress the profibrinolytic protein under the control of a tac promoter. Almost all the recombinant STK was exported to the periplasmic space and recovered after gentle lysozyme digestion of induced cells. The periplasmic fraction was chromatographed on DEAE Sepharose followed by chromatography on phenyl-agarose. Active proteins eluted between 4.5 and 0% ammonium sulfate, when a linear gradient was applied. Three major STK derivatives of 47.5 kDa, 45 kDa and 32 kDa were detected by Western blot analysis with a polyclonal antibody. The 32-kDa protein formed a complex with human plasminogen but did not exhibit Glu-plasminogen activator...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Recombinant streptokinase; Plasminogen activators; Protein purification.
Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001200007
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Modulation of staphylokinase-dependent plasminogen activation by mono- and divalent ions BJMBR
Yarzábal,A.; Serrano,R.L.; Puig,J..
The effect of several ions (Cl-, Na+, K+, Ca2+) on the rate of plasminogen (Pg) activation by recombinant staphylokinase (rSTA) is reported. Both monovalent and divalent ions affect the rate at which Pg is activated by rSTA, in a concentration-dependent manner (range 0-100 mM). In almost all cases, a decrease of the initial velocity of activation was observed. Cl- showed the most striking inhibitory effect at low concentrations (64% at 10 mM). However, in the presence of a fibrin surface, this inhibition was attenuated to 38%. Surprisingly, 10 mM Ca2+ enhanced the Pg activation rate 21% when a polymerized fibrin matrix was present. These data support the idea that ions can modulate the rate of Pg activation through a mechanism that may be associated with...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Staphylokinase; Plasminogen activation; Fibrinolysis.
Ano: 1999 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000100005
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