Esterase Activity of Serum Albumin Studied by ¹H NMR Spectroscopy and Molecular Modelling.

ABSTRACT: Serum albumin possesses esterase and pseudo-esterase activities towards a number of endogenous and exogenous substrates, but the mechanism of interaction of various esters and other compounds with albumin is still unclear. In the present study, proton nuclear magnetic resonance (¹H NMR) has been applied to the study of true esterase activity of albumin, using the example of bovine serum albumin (BSA) and p-nitrophenyl acetate (NPA). The site of BSA esterase activity was then determined using molecular modelling methods. According to the data obtained, the accumulation of acetate in the presence of BSA in the reaction mixture is much more intense as compared with the spontaneous hydrolysis of NPA, which indicates true esterase activity of albumin towards NPA. Similar resul

SUBMITTER: Belinskaia DA 

PROVIDER: S-EPMC8508922 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature