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|title: ||Unfolding of cardosin A in organic solvents and detection of intermediaries|
|authors: ||Sarmento, Ana Cristina|
Oliveira, Cláudia S.
Esteves, Valdemar I.
Moir, Arthur J.G. Moir
|keywords: ||Aspartic proteinases|
|issue date: ||2009|
|abstract: ||In the present study the relationship between conformational stability and enzymatic activity in the
presence of organic solvents (OS) was investigated. We have found that cardosin A, the model protease
investigated in this work, inactivates through a biphasic mechanism, which is incipient in aqueous buffer
and becomes visible in the presence of hydrophilic OS. In fact, in OS this inactivation originates stable intermediaries
thatwere detected in acetonitrile. This biphasic mechanism can be described in two phases: an
initial one, where OS induce alterations that affect the active site cleft and global mobility, but with little
interference on the global protein conformation, and, a second phase, where there is a global change in
protein conformation with concomitant activity loss. It is shown that in the presence of hydrophilic OS
there is a larger mobility of the enzyme, revealed by limited proteolysis, probably due to a weakening of
hydrophobic interactions within the protein core.|
|publisher version/DOI: ||http://dx.doi.org/10.1016/j.molcatb.2008.08.004|
|source: ||Journal of Molecular Catalysis B: Enzymatic|
|appears in collections||DQ - Artigos|
QOPNA - Artigos
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