Nonserine esterases from rat liver cytosol

Dong Hyun Kim; Yuh-Shyong Yang; William B. Jakoby

doi:10.1016/1046-5928(90)90040-6

Nonserine esterases from rat liver cytosol

Dong Hyun Kim^*, Yuh-Shyong Yang, William B. Jakoby

^*Corresponding author for this work

Department of Biological Science and Technology

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

An effort to identify the major general esterases of rat liver cytosol that are insensitive to the serine esterase inhibitor paraoxon (diethyl 4-nitrophenyl phosphate) has led to the isolation of a dozen enzymes. Four of these are electrophoretically homogeneous. Although purified on the basis of their hydrolytic activity toward 4-nitrophenyl acetate, each of the enzymes has a very broad and overlapping substrate specificity for aromatic esters. Thiol esters serve as substrates but, within the limits of the methods used, amides are not hydrolyzed.

Original language	English
Pages (from-to)	19-27
Number of pages	9
Journal	Protein Expression and Purification
Volume	1
Issue number	1
DOIs	https://doi.org/10.1016/1046-5928(90)90040-6
State	Published - Sep 1990

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AU - Jakoby, William B.

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AB - An effort to identify the major general esterases of rat liver cytosol that are insensitive to the serine esterase inhibitor paraoxon (diethyl 4-nitrophenyl phosphate) has led to the isolation of a dozen enzymes. Four of these are electrophoretically homogeneous. Although purified on the basis of their hydrolytic activity toward 4-nitrophenyl acetate, each of the enzymes has a very broad and overlapping substrate specificity for aromatic esters. Thiol esters serve as substrates but, within the limits of the methods used, amides are not hydrolyzed.

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Nonserine esterases from rat liver cytosol

Abstract

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