Pseudo-esterase Activity of Human Albumin: SLOW TURNOVER ON TYROSINE 411 AND STABLE ACETYLATION OF 82 RESIDUES INCLUDING 59 LYSINES

Human albumin is thought to hydrolyze esters because multiple equivalents of product are formed for each equivalent of albumin. Esterase activity with p-nitrophenyl acetate has been attributed to turnover at tyrosine 411. However, p-nitrophenyl acetate creates multiple, stable, acetylated adducts, a...

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Detalhes bibliográficos
Main Authors: Lockridge, Oksana, Xue, Weihua, Gaydess, Andrea, Grigoryan, Hasmik, Ding, Shi-Jian, Schopfer, Lawrence M., Hinrichs, Steven H., Masson, Patrick
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2008
Assuntos:
Enzyme Catalysis and Regulation
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2504902/
https://ncbi.nlm.nih.gov/pubmed/18577514
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M802555200
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