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Acetylation of human serum albumin by <i>p<\/i>-nitrophenyl acetate. <i>Biochemistry<\/i>, <b>14<\/b>, 4989\u20134994 (1975).","DOI":"10.1021\/bi00693a031"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9) Ikeda K, Kurono Y, Ozeki Y, Yotsuyanagi T. Effects of drug bindings on esterase activity of human serum albumin. Dissociation constants of the complexes between the protein and drugs such as <i>N<\/i>-arylanthranilic acids, coumarin derivatives and prostaglandins. <i>Chem. Pharm. Bull.<\/i>, <b>27<\/b>, 80\u201387 (1979).","DOI":"10.1248\/cpb.27.80"},{"key":"10","unstructured":"10) Lockridge O, Xue W, Gaydess A, Grigoryan H, Ding SJ, Schopfer LM, Hinrichs SH, Masson P. Pseudo-esterase activity of human albumin: slow turnover on tyrosine 411 and stable acetylation of 82 residues including 59 lysines. <i>J. Biol. Chem.<\/i>, <b>283<\/b>, 22582\u201322590 (2008)."},{"key":"11","doi-asserted-by":"crossref","unstructured":"11) Kurono Y, Kushida I, Tanaka H, Ikeda K. 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