A genetically controlled esterase in rat plasma

Augustinsson, Klas‐Bertil; Henricson, B.

doi:10.1016/0304-4165(66)90195-4

Cited by 46 publications

(7 citation statements)

References 20 publications

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“…The main part of the arylesterase activity migrated with the albumin fraction, a minor part was found in the prealbumin region. Augustinsson and Henricson (1966) found a fraction in rat plasma which migrated faster than albumin in starch gel electrophoresis and hydrolyzed anapthylacetate, -propionate and -butyrate. Also Segonzak (1963,1964) detected arylesterase activity (substrates: phenylacetate resp.…”

Section: Electrophoretic Differentiationmentioning

confidence: 98%

The human serum paraoxonase—Polymorphism and specificity

Mallinckrodt¹,

Diepgen

1988

Toxicological & Environmental Chemistry

111

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Human serum contains EDTA-sensitive (Ca ++ -dependent) and EDTA-stable (albumin) paraoxonases which hydrolyse paraoxon, 0,0-diethyl,0-4-nitrophenyl phosphate.In Caucasians the EDTA-sensitive enzyme shows a genetically determined polymorphism which is governed by two alleles. In typical Mongoloid or Negro populations this polymorphism is expressed to a lesser degree, and in a few samples (e.g. Aborigines) it cannot be observed at all. The distribution of the activity of the EDTAstable (albumin) paraoxonase is unimodal.Many authors supposed that paraoxonase is an arylesterase (EC 3.1.1.2) which means that it is also able to hydrolyse phenylacetate or β-naphthylacetate. New investigations have shown that the human serum fractions splitting paraoxon can be separated from those hydrolysing phenylacetate and related substrates.The polymorphism of the EDTA-sensitive human serum paraoxonase can be applied to investigations concerning specificity. From this it becomes evident that this enzyme is rather specific. Already slight changes of the paraoxon molecule lead to a decrease of activity. On the other hand the enzyme seems to hydrolyse also phosphonic acid esters and 4-nitrophenylacetate in the same way like paraoxon (polymorphism).There is a linkage relationship of paraoxonase with cystic fibrosis and DNA markers. According to these results the (EDTA-sensitive) paraoxonase locus is on the human chromosome 7.A high serum paraoxonase level actually protects serum cholinesterase (EC 3.1.1.8) and has to be considered in biological monitoring of workers exposed to parathion.

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Section: Electrophoretic Differentiationmentioning

confidence: 98%

The human serum paraoxonase—Polymorphism and specificity

Mallinckrodt¹,

Diepgen

1988

Toxicological & Environmental Chemistry

111

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“…Other biochemical loci were characterized using the following methods: Acon-1 (Adams et aL, 1984), Ahd-2 (Adams et al, 1984), Es-1 (Augustinsson and Henricson, 1966), Es-3 (Womack, 1972), Fh (Erikson et al, 1976), Gc (Bender et al, 1981), Hao-1 (Cramer et al, 1986), Hbb (French and Roberts, 1965), Mup-1 (Nikaido et al, 1982), Pep-3 (Womack and Cramer, 1980), Pg-1 (Kondo and Yamada, 1983a), Pg-2 , Svp-1 (Gasser, 1972), and R T1 (Natori et al, 1981). Genotypes at the h and p loci were determined visually.…”

Section: Other Biochemical and Coat-color Locimentioning

confidence: 99%

Genetic polymorphism of tear proteins in the rat

et al. 1988

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Polymorphism of tear proteins was found by agarose gel electrophoresis among inbred strains of rats. The proteins (RTP-1) are inherited as a single autosomoal trait. The locus was designated Rtp-1 (rat tear protein-1) and it had two codominant alleles (Rtp-1a, Rtp-1b). Although we did not find any recombinant between the Rtp-1 and the Mup-1 loci among 67 backcross progeny, we found 3 strains with the recombinant type between them in 33 inbred strains tested. The results suggest that the Rtp-1 locus is very closely linked with the Mup-1 locus, which belongs to rat linkage group II. RTP-1 proteins strongly reacted with anti-MUP-1 A serum on agarose gel electrophoretograms.

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“…This esterase is called esterase-1 (ES-1) and occurs predominantly in the intestine, intestinal lymph and plasma [4]. Although ES-1 was first described in plasma by Augustinsson and Henricson as early as 1966 [5], there is no specific assay to determine rat plasma ES-1 activity, which also holds for most other esterases. This is because the physiological substrates of these enzymes are unknown and artificial substrates do not discriminate between esterases.…”

Section: Introductionmentioning

confidence: 99%

Determination of rat plasma esterase‐1 (ES‐1) activity by scanning densitometry of gradient polyacrylamide gels with zymogram detection

et al. 1991

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There is no specific assay for rat plasma esterase-1 (ES-1) activity. Plasma contains many esterases, while known substrates do not discriminate between esterases. With gel electrophoresis, plasma esterase isozymes can be separated. Thus, a method consisting of gradient polyacrylamide gel electrophoresis, visualization of the enzyme with a staining technique based on substrate conversion, and densitometric scanning of the stained gel has been developed for quantitative measurement of rat plasma ES-1 activity. ES-1 activities were expressed as total peak areas. Reproducibility of the method was found to be about 10% (expressed as apparent between-gel coefficient of variation). When the ES-1 zone areas was expressed relative to that of a plasma ES-1 standard, reproducibility was about 3%. The kinetics of catalysis of alpha-naphthyl acetate hydrolysis by ES-1 could be determined with the gel scanning assay; the Km was 0.76 mM. At the alpha-naphthyl acetate concentration of 2.69 mM, total peak areas of the ES-1 zone were linearly associated with the staining time (up to at least 40 min) and amount of plasma (up to 26.25 microL). The pH of the staining buffer influences the ES-1 zone area, the largest areas being obtained when the pH ranged between 7.0 and 7.8. With propionate as acyl moiety of the alpha-naphthyl ester substrate, ES-1 zone areas were higher than with either acetate, butyrate or hexanoate.

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A genetically controlled esterase in rat plasma

Cited by 46 publications

References 20 publications

The human serum paraoxonase—Polymorphism and specificity

The human serum paraoxonase—Polymorphism and specificity

Genetic polymorphism of tear proteins in the rat

Determination of rat plasma esterase‐1 (ES‐1) activity by scanning densitometry of gradient polyacrylamide gels with zymogram detection

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