Pseudo-esterase Activity of Human Albumin
نویسندگان
چکیده
منابع مشابه
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 property contrary to turnover. Our goal was to identify residues that become acetylated by p-nit...
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متن کاملRole of arg-410 and tyr-411 in human serum albumin for ligand binding and esterase-like activity.
Recombinant wild-type human serum albumin (rHSA), the single-residue mutants R410A, Y411A, Y411S and Y411F and the double mutant R410A/Y411A were produced using a yeast expression system. The recombinant proteins were correctly folded, as they had the same stability towards guanidine hydrochloride and the same CD spectrum as HSA isolated from serum (native HSA). Thus the global structures of th...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2008
ISSN: 0021-9258
DOI: 10.1074/jbc.m802555200