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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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| Autori principali: | , , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Biochemistry and Molecular Biology
2008
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| Soggetti: | |
| Accesso online: | 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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