Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria

Aeromonas sobria Released from Production of C5a by ASP, a Serine Protease

Impaired plasma clottability induction through fibrinogen degradation by ASP, a serine protease released from Aeromonas sobria

Aeromonas sobria infection often advances to sepsis, in which interaction of bacterial components with plasma proteins possibly causes various disorders. This bacterium releases a serine protease (ASP), a putative virulence factor, and binds to fibrinogen. To study the ASP effect on fibrinogen, we incubated fibrinogen or plasma with ASP and investigated their clotting elicited by thrombin, whic...

Involvement of the Arg566 residue of Aeromonas sobria serine protease in substrate specificity

Aeromonas sobria serine protease (ASP) is an extracellular serine protease secreted by the organism. Here, we identified the amino acid residue of ASP that contributes to substrate specificity by using both synthetic peptides and biological protein components. The results showed that the arginine residue at position 566 (Arg-566) of ASP, which is located in the extra occluding region of ASP clo...

investigating the integration of translation technologies into translation programs in iranian universities: basis for a syllabus design in translation technology

today, information technology and computers are indispensable tools of any profession and translation technologies have become an indispensable part of translator’s workstation. with the increasing demands for high productivity and speed as well as consistency and with the rise of new demands for translation and localization, it is necessary for translators to be familiar with market demands an...

a structural survey of the polish posters

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