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Electrostatic compared with hydrophobic interactions between bovine serum amine oxidase and its substrates.

A steady-state kinetic study of bovine serum amine oxidase activity was performed, over a wide range of pH values (5.4-10.2) and ionic strength (10-200 mM), using various (physiological and analogue) substrates as specific probes of the active-site binding region. Relatively small changes in k (cat)...

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Sonraí Bibleagrafaíochta
Main Authors: Di Paolo, Maria Luisa, Stevanato, Roberto, Corazza, Alessandra, Vianello, Fabio, Lunelli, Lorenzo, Scarpa, Marina, Rigo, Adelio
Formáid: Artigo
Teanga:Inglês
Foilsithe: 2003
Ábhair:
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC1223303/
https://ncbi.nlm.nih.gov/pubmed/12529179
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20021055
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