Ligand binding to the FA3-FA4 cleft inhibits the esterase-like activity of human serum albumin.

Ligand binding to the FA3-FA4 cleft inhibits the esterase-like activity of human serum albumin.

The hydrolysis of 4-nitrophenyl esters of hexanoate (NphOHe) and decanoate (NphODe) by human serum albumin (HSA) at Tyr411, located at the FA3-FA4 site, has been investigated between pH 5.8 and 9.5, at 22.0°C. Values of Ks, k+2, and k+2/Ks obtained at [HSA] ≥ 5×[NphOXx] and [NphOXx] ≥ 5×[HSA] (Xx is...

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Bibliographic Details
Main Authors: Paolo Ascenzi, Loris Leboffe, Alessandra di Masi, Viviana Trezza, Gabriella Fanali, Magda Gioia, Massimo Coletta, Mauro Fasano
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4366387?pdf=render

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http://europepmc.org/articles/PMC4366387?pdf=render

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