A hydrolytic enzymelike behavior or bovine serum albumin in hydrolysis of p-nitrophenyl esters

…, T Uchida, S Tanimoto, M Okano, T Sugimoto

Index: Kokubo, Toshio; Uchida, Toshio; Tanimoto, Shigeo; Okano, Masaya; Sugimoto, Toyonari Tetrahedron Letters, 1982 , vol. 23, # 15 p. 1593 - 1596

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Citation Number: 24

Abstract

Abstract The investigation of hydrolysis of p-nitrophenyl acetate (NPA) catalyzed by bovine serum albumin (BSA) proved that the initial rate in the steady state folows a Michaelis- Menten equation. In the use of D-and Lp-nitrophenyl α-methoxyphenlacetates (D-and L- NPMA's) as an enantiomeric ester, the L-enantiomer is hydrolyzed about three times faster than the D-enantiomer, mainly due to stronger binding of the former enantiomer by BSA.

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