Aspirin hydrolyzing esterases from rat liver cytosol

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

doi:10.1016/0006-2952(90)90546-W

Aspirin hydrolyzing 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

18 Scopus citations

Abstract

Unlike most esterases, which are predominantly bound to the microsomal fraction, the enzymes hydrolyzing acetylsalicylic acid are present in an equal amount in the cytosol. Two soluble isozymes were purified to homogeneity from rat liver and characterized as serine esterases with a M_r, of 35,000. Both had the wide substrate spectrum characteristic of enzymes active in detoxication. Both had a very low K_m for acetylsalicylate. Three other cytoplasmic enzymes active with aspirin were observed but these differed in their high M_r (about 220,000) and their lack of reactivity with antibody to one of the homogeneous isozymes.

Original language	English
Pages (from-to)	481-487
Number of pages	7
Journal	Biochemical Pharmacology
Volume	40
Issue number	3
DOIs	https://doi.org/10.1016/0006-2952(90)90546-W
State	Published - 1 Aug 1990

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title = "Aspirin hydrolyzing esterases from rat liver cytosol",

abstract = "Unlike most esterases, which are predominantly bound to the microsomal fraction, the enzymes hydrolyzing acetylsalicylic acid are present in an equal amount in the cytosol. Two soluble isozymes were purified to homogeneity from rat liver and characterized as serine esterases with a Mr, of 35,000. Both had the wide substrate spectrum characteristic of enzymes active in detoxication. Both had a very low Km for acetylsalicylate. Three other cytoplasmic enzymes active with aspirin were observed but these differed in their high Mr (about 220,000) and their lack of reactivity with antibody to one of the homogeneous isozymes.",

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T1 - Aspirin hydrolyzing esterases from rat liver cytosol

AU - Kim, Dong Hyun

AU - Yang, Yuh-Shyong

AU - Jakoby, William B.

PY - 1990/8/1

Y1 - 1990/8/1

N2 - Unlike most esterases, which are predominantly bound to the microsomal fraction, the enzymes hydrolyzing acetylsalicylic acid are present in an equal amount in the cytosol. Two soluble isozymes were purified to homogeneity from rat liver and characterized as serine esterases with a Mr, of 35,000. Both had the wide substrate spectrum characteristic of enzymes active in detoxication. Both had a very low Km for acetylsalicylate. Three other cytoplasmic enzymes active with aspirin were observed but these differed in their high Mr (about 220,000) and their lack of reactivity with antibody to one of the homogeneous isozymes.

AB - Unlike most esterases, which are predominantly bound to the microsomal fraction, the enzymes hydrolyzing acetylsalicylic acid are present in an equal amount in the cytosol. Two soluble isozymes were purified to homogeneity from rat liver and characterized as serine esterases with a Mr, of 35,000. Both had the wide substrate spectrum characteristic of enzymes active in detoxication. Both had a very low Km for acetylsalicylate. Three other cytoplasmic enzymes active with aspirin were observed but these differed in their high Mr (about 220,000) and their lack of reactivity with antibody to one of the homogeneous isozymes.

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U2 - 10.1016/0006-2952(90)90546-W

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JF - Biochemical Pharmacology

IS - 3

ER -

Aspirin hydrolyzing esterases from rat liver cytosol

Abstract

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