Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1991 Jan-Feb;19(1):100-6.

Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities

K N Gan  1 , A Smolen, H W Eckerson, B N La Du
Affiliations
  • PMID: 1673382

Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities

K N Gan et al. Drug Metab Dispos. 1991 Jan-Feb.

Abstract

Evidence is presented that human serum contains a single enzyme with both paraoxonase and arylesterase activities. Throughout the steps of purification and after obtaining over 600-fold purification of the enzyme, the arylesterase activity (measured with phenylacetate as the substrate) co-eluted and retained the same ratio of activity to paraoxonase activity as it had in the initial plasma sample. Paraoxon and DFP (diisopropylfluorophosphate) both complete with phenylacetate as substrates; the inhibition is of mixed type with paraoxon and competitive with DFP. Paraoxonase and arylesterase activities require calcium, and both are inhibited to the same degree by EDTA. Purified arylesterase/paraoxonase is a glycoprotein with a minimal molecular weight of about 43,000. It has up to three sugar chains per molecule, and carbohydrate represents about 15.8% of the total weight. The enzyme has an isoelectric point of 5.1. Its amino acid composition shows nothing unusual, except for a relatively high content of leucine. We conclude that human serum arylesterase and paraoxonase activities are catalyzed by a single enzyme, capable of hydrolyzing a broad spectrum of organophosphate substrates and a number of aromatic carboxylic acid esters. Studies on the genetically determined polymorphism responsible for two allozymic forms (A and B) of the esterase are described in the following paper.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

Publication types

LinkOut - more resources