Nicotinate esters: their binding to and hydrolysis by human serum albumin.
Nicotinate esters were studied for their binding to, and hydrolysis by, human serum albumin. Some esters (ethyl, isopropyl, t-butyl, cyclohexyl, benzyl) were bound but not hydrolysed, while others (2-chloroethyl, 2-butoxyethyl) displayed the opposite behaviour; 1-carbamoylethyl ester was neither bound nor readily hydrolysed. Only p-methoxyphenyl nicotinate was both a ligand and a substrate, and its rate constants of binding and hydrolysis were calculated in a stepwise procedure using a kinetic model.
School of Pharmacy, University of Lausanne, Switzerland.
A
A
Steiner
J M
JM
Mayer
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B
Testa
D002851:Chromatography, High Pressure Liquid; D003956:Dialysis; D006801:Humans; D006868:Hydrolysis; D008954:Models, Biological; D009539:Nicotinic Acids / Q000378:metabolism* / Q000493:pharmacokinetics; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet
D009539:Nicotinic Acids; D012709:Serum Albumin