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At least 793 records · Page 44Linked to original sources
PubMed1986

Alteration of in vivo and in vitro effects of heroin by esterase inhibition.

Selective inhibition of peripheral esterases by tri-ortho-tolyl phosphate in the mouse resulted in an increase in the analgetic activity of heroin, without affecting the activity of morphine. In vitro inhibition of esterases by paraoxon reduced the affinity of heroin for the opiate receptor, while that of morphine was unaffected. These results suggest that both central and peripheral esterases are involved in the metabolism of heroin and that interference with critical esterases can alter its pharmacologic and toxicologic effects.

Acetates↗
PubMed1987

Involvement of the esterase active site of egasyn in compartmentalization of beta-glucuronidase within the endoplasmic reticulum.

Organophosphorous compounds, which are potent inhibitors of egasyn-esterase activity, caused a rapid dissociation of the high molecular weight egasyn-microsomal beta-glucuronidase complex when administered in vivo or when added in vitro to microsomal suspensions. The dissociation was relatively specific to phosphodiester inhibitors of the esterase active site. Also, the egasyn-esterase active site was inaccessible to substrates and to inhibitors when egasyn was complexed to beta-glucuronidase. Dissociation of the egasyn-microsomal beta-glucuronidase complex in vivo by organophosphorous compounds was followed by massive and rapid secretion of microsomal beta-glucuronidase, but not egasyn, into plasma. These experiments implicate the egasyn-esterase active site in attachment of microsomal beta-glucuronidase to egasyn by a novel mechanism that, in turn, compartmentalizes beta-glucuronidase within the endoplasmic reticulum.

Animals↗
PubMed1990

Comparison of roles of serine esterase in chicken and human natural cytotoxicity.

The requirements for serine esterase activity in the spontaneous cell-mediated cytotoxicity of human lymphocytes and chicken granulocytes have been compared. The lysis of K-562 target cells and of LSCC-H32 chicken target cells was prevented by the serine esterase inhibitor TPCK. ATEE, the substrate of chymotrypsin, impaired both cytotoxic reactions, but to a lesser degree the cytotoxicity of chicken granulocytes. TPCK inhibited the "trigger" mechanism in an early calcium-dependent step and later calcium-independent events in both systems. However, calcium-independent lysis was depressed by serine esterase inhibitor only in the avian cytotoxicity. These findings suggest that avian target cell cytolysis consists of similar sequential phases to those already demonstrated in the human NK cell reaction, and serine esterase is required during several stages of cytotoxicity in the avian system.

Animals↗
PubMed1992

Coenzyme A- and NADH-dependent esterase activity of methylmalonate semialdehyde dehydrogenase.

Methylmalonate semialdehyde dehydrogenase purified to homogeneity from rat liver possesses, in addition to its coupled aldehyde dehydrogenase and CoA ester synthetic activity, the ability to hydrolyze p-nitrophenyl acetate. The following observations suggest that this activity is an active site phenomenon: (a) p-nitrophenyl acetate hydrolysis was inhibited by malonate semialdehyde, substrate for the dehydrogenase reaction; (b) p-nitrophenyl acetate was a strong competitive inhibitor of the dehydrogenase activity; (c) NAD+ and NADH activated the esterase activity; (d) coenzyme A, acceptor of acyl groups in the dehydrogenase reaction, accelerated the esterase activity; and (e) the product of the esterase reaction proceeding in the presence of coenzyme A was acetyl-CoA. These findings suggest that an S-acyl enzyme (thioester intermediate) is likely common to both the esterase reaction and the aldehyde dehydrogenase/CoA ester synthetic reaction.

Aldehyde Oxidoreductases↗
PubMed1995

An acetylglucomannan esterase of Aspergillus oryzae; purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan.

An acetyl glucomannan esterase (AGME) was purified to electrophoretic homogeneity from the culture supernatant of Aspergillus oryzae. This new enzyme had a molecular mass of 36 kDa and an isoelectric point of 4.6. It was most active in the pH range 5.0-5.5 and was stable for 24 h at 40 degrees C at pH 5.0-6.0. The purified esterase liberated acetic acid from O-acetyl-galactoglucomannan, O-acetyl-4-O- methylglucuronoxylan and alpha-naphtyl acetate. The specific activity was 10-times higher for acetylated mannan than for acetylated xylan. The enzyme was able to act on polymeric substrate but activity was clearly enhanced by addition of mannanase from Trichoderma reesei and alpha-galactosidase from guar seeds. Presence of mannanase also increased the liberation of acetic acid in long-term hydrolysis (24 h), while the addition of alpha-galactosidase had no effect. No significant synergism between these two glycanases and the previously characterized esterase of A. oryzae (FE), which is also able to deacetylate galactoglucomannan, was observed. Even though the AGME had 8-times higher specific galactomannan deacetylating activity than the FE, the maximum amount of acetic acid liberated from the polymeric galactoglucomannan by AGME was only 80% of that of FE. Both esterases clearly enhanced the action of mannanase and alpha-galactosidase in the degradation of O-acetyl-galactoglucomannan isolated from Norway spruce.

Aspergillus oryzae↗
PubMed1983

The effect of intestinal esterase inhibition on the in vivo absorption and toxicity of Di-n-butyl phthalate.

Inhibition of intestinal mucosal esterases by S,S,S-tributylphosphorotrithioate (DEF) did not alter the gastro-intestinal absorption of di-n-butyl phthalate (DBP) in the rat. After intragastric administration of [14C]DBP to control and esterase-inhibited animals, the disappearance of 14C from the small intestine and the levels of 14C in the blood were not significantly different in the two groups over the first 4 hr. Peak blood levels of 14C occurred 2 hr after dosing in both groups of rats. The circulating [14C]butyl phthalate in the diester form accounted for less than 5% of the total 14C at 2 hr, regardless of intestinal esterase activity. The remaining 14C was associated with mono-n-butyl phthalate or more polar metabolites. These data suggest an important role for pancreatic esterases, which may be protected from DEF-mediated inhibition by storage in zymogen granules, in the metabolism and absorption of DBP.

Animals↗
PubMedDate not supplied

Age-dependent changes in juvenile hormone esterase and general carboxyesterase activity in the hemolymph of the colorado potato beetle, Leptinotarsa decemlineata.

An in vitro method has been developed for the quantitative estimation of juvenile hormone (JH) esterase activity in the hemolymph of the Colorado beetle Leptinotarsa decemlineata Say. The apparent Km value for JH-esterase was determined. JH-esterase and general carboxyesterase activities were estimated throughout the life cycle and under different photoperiodic conditions. High activities were observed in fourth instar larvae and in beetles just before diapause. Lower activities were found in third instar larvae, long-day, diapause and post-diapause beetles. Similar variations were found in general carboxyesterase activity but not in protein concentration. A possible role for the esterase in the regulation of the JH titer is discussed.

Aging↗
PubMed1977

Sex differences in the pattern of esterase-active antigens in microsomes from various rat strains.

Esterase-active antigens present in male and female liver microsomes isolated from three different rat strains-(Sprague-Dawley, Wistar and Dark Agouti) were characterized in crossed immunoelectrophoresis in combination with a zymogram method for esterase activity. No qualitative but some quantitative differencies were encountered between the sexes. Thus, two out of ten antigens were present in significantly lower and one in significantly higher concentrations in male than in female microsomes, demonstrating that although the overall esterase activity in liver may be similar for males and females, the concentration of the individual antigens does vary between the sexes. No qualitative or quantitative differences in the pattern of esterase-active antigens were found between the different strains.

Animals↗
PubMed1978

The evidence for the existence of chymotrypsin-like esterase activity in the plasma membranes of rabbit neutrophils and the specific chemotactic peptide binding activity of the subcellular fractions.

1. Light- and heavy-plasma membrane fractions have been isolated from rabbit neutrophils and a chymotrypsin-like esterase has been shown to be present in these fractions. 2. The molecular weight of the chymotrypsin-like esterase of rabbit neutrophil plasma membrane was estimated to be about 200 000. 3. About 93% of the chymotrypsin-like esterase of the plasma membranes is esterase 1 and the susceptibility to potential inhibitors was similar in light- and heavy-plasma membrane. 4. Chemotactic peptide, [3H]formyl-norleucyl-leucyl-phenylalanine [3H]formyl-Nle-Leu-Phe) binding by subcellular fractions shows that the highest specific binding was observed in the light-plasma membrane was about 2-fold higher than the heavy-plasma membrane, about 37-fold higher than the nuclear fraction, about 3-fold higher than lysosomal fraction and about 10-fold higher than the microsomal fraction.

Animals↗
PubMed1978

Electrophoretic separation of esterases of Alaria marcianae (La Rue, 1917) (Trematoda).

1. Disc electrophoresis was used to determine the esterase isoenzymes present in adults of the strigeoid trematode Alaria marcianae (La Rue, 1917). 2. Eight esterase bands were found with alpha-naphthyl acetate as the substrate and Fast Blue RR as the dye. 3. From results obtained with inhibitors, four different types of esterases were tentatively identified; cholinesterase (one band), ali-esterase or B-type (one band), arylesterase or A-type (2 bands) and acetylesterase or C-type (4 bands).

Animals↗
PubMed1986

Variations in the serum esterases of chimpanzees.

Seventy chimpanzees, representing Pan paniscus (the pygmy chimp) and all four races of the common chimpanzee (Pan troglodytes), were examined for electrophoretic variation in their serum esterases. Only three variant electromorphs were observed at these six loci. One of these was at the albumin-associated esterase locus, and the other two were at esterase 4. This is the first report of any variation in an esterase or albumin in chimpanzees.

Animals↗
PubMed1988

Cholesterol esterases from normal and FEC hamster liver.

1. Synthetic cholesteryl esters with various acyl chain length (C2-C18) are hydrolysed by several enzymes in hamster liver. 2. The comparison of effect of inhibitors, divalent cations, detergents, pH and substrate specificity allows discrimination between four enzymes hydrolyzing cholesteryl esters, which are characterized by their enzymatic properties, two cholesterol esterases (resistant to E600) hydrolyzed medium- and long-chain cholesteryl esters, whereas short-chain cholesteryl esters were hydrolyzed by two different carboxylesterases (dramatically inhibited by E600). 3. The acid cholesterol esterase (identical to the lysosomal lipase) exhibited a pH optimum at pH 5.0 and is activated by 1 mM taurocholate. 4. The alkaline cholesterol esterase (pH optimum 7.5) is not very sensitive to the tested effectors. 5. Both acid and alkaline carboxylesterases (pH optima 5.5 and 7.5), were characterized by their strict dependence on divalent cations (Mn2+ or Mg2+). 6. The acid carboxylesterase was inhibited by increasing concentrations of Triton X-100, whereas the alkaline carboxylesterase was dramatically activated by 2 g/l Triton X-100. 7. No significant difference was observed in activities of cholesterol esterases or carboxylesterases between normal and FEC hamster livers.

Animals↗
PubMed1989

Physicochemical characterization and tissue distribution of esterases in two salamandridae species (Mertensiella luschani and Salamandra salamandra).

1. Tissue- and species-specificity of the electrophoretic patterns of the multiple molecular forms of esterases were observed in the urodele amphibians Mertensiella luschani luschani, M.l. helverseni and Salamandra salamandra. All esterases--distributed into two electrophoretic mobility areas in gonads, muscles and brain and into four areas in liver, stomach and intestine--were characterized as carboxylesterases. 2. M. l. luschani and S. salamandra liver esterases were electrofocused into nine and eleven major bands with pIs ranging from 4.60 to 5.65 and from 4.40 to 6.20, respectively. 3. Two size groups of esterases were observed in liver extracts of the above three subspecies by Sephadex G-200 gel filtration. The mean values of their apparent molecular weights were 70,000 and 230,000 respectively.

Animals↗
PubMed1989

Esterases in natural populations of normal and Echinostoma revolutum-infected Helisoma trivolvis (Gastropoda).

Esterases of the digestive gland-gonad (DGG) complex of individual snails from a wild population of Helisoma trivolvis infected with the trematode Echinostoma revolutum were analyzed by vertical slab PAGE and compared to similar DGG homogenates of uninfected conspecifics from the same population. Our analysis indicated that: 1. Four classes of esterases, some atypical, could be resolved using diagnostic inhibitors. 2. Uninfected snails demonstrated polymorphism for two of these four esterase groups, including cholinesterases (CHE), in the 34 individual DGGs analyzed. 3. The rarer of the two ChE phenotypes in the uninfected sample (29.4%) was present in 100% of the 17 infected snails examined. However, no changes in esterase zymograms of infected DGGs due to the parasite were noted. 4. The possibility that the 'rare' ChE phenotype is somehow related to host susceptibility to Echinostoma revolutum is discussed in view of similar apparent linkages in other snail-trematode systems.

Animals↗
PubMed1993

Esterases in quail (Coturnix coturnix). Physicochemical and developmental aspects.

1. Soluble esterases of digestive system organs of various developmental stages in the quail (Coturnix coturnix) were resolved by polyacrylamide gel electrophoresis into several molecular forms which were characterized as carboxylesterases, acetylesterases, cholinesterases and esterases sensitive to eserine. 2. The pI of the majority of esterasic activity in several quail and chicken tissues was observed in the range of 5.1-5.6, while the apparent molecular weight in liver extracts was 60,000. 3. The expression of the esterase multiple molecular forms was found to be both tissue- and developmental stage-specific, with electrophoretic patterns becoming more complex in number and/or staining intensity upon hatching and thereafter, especially in liver and intestine.

Acetylesterase↗
PubMed1990

Epidemiological typing of Acinetobacter strains by esterase electrophoresis.

Fifty-three strains of Acinetobacter, belonging to the species A baumannii, A. haemolyticus and A. johnsonii, were differentiated by electrophoretic typing of their esterases, on the basis of both the enzyme specific activity profiles and their electrophoretic mobilities. Each esterase was defined by its spectrum of hydrolytic activity toward five synthetic substrates and its sensitivity to di-isopropyl fluorophosphate. Since each enzyme was not detected in all strains of a given species, several zymotypes could be defined by the patterns of combinations of esterases. Thus, 24 zymotypes were defined in the 32 A. baumannii strains, 4 were defined in the 10 A. haemolyticus strains and 6 were defined in the 11 A. johnsonii strains. When the electrophoretic mobilities of the various esterases were included, each of the 53 strains of Acinetobacter (with the exception of three A. haemolyticus strains) showed a distinct electrotype.

Acinetobacter↗
PubMed1991

Pseudomonas aeruginosa isolate typing by esterase electrophoresis.

Esterase electrophoretic typing was used to classify clinical isolates of Pseudomonas aeruginosa. One hundred and twenty-seven P. aeruginosa strains belonging to 16 serotypes (including 16 non-typeable strains) and isolated from diverse human infections in three hospitals, and the type strain ATCC 10 145, were tested. Four main kinds of esterase and 4 additional esterases were distinguished by their spectra of hydrolytic activity toward synthetic substrates and by their sensitivity or resistance to di-isopropyl fluorophosphate. The electrophoretic variations of these enzymes were used to define 42 zymotypes. Electrophoretic typing of esterase appeared to be more sensitive than serotyping and the results of the two methods did not correlate. When the two typing methods were used in parallel, 78 different combinations of serotype and zymotype were obtained.

Bacterial Typing Techniques↗
PubMed1995

Molecular aspects of carboxylesterase isoforms in comparison with other esterases.

The involvement of carboxylesterase, acetylcholinesterase, butyrylcholinesterase and cholesterol esterase in pharmacology and toxicology are well recognized. However, there are few papers concerning the comparative studies of these serine hydrolases in terms of molecular level. Recently, we have studied various aspects of carboxylesterases using cDNAs of carboxylesterase isozymes purified from 9 animal species and human liver microsomes, and found that there is high homology of the N-terminal amino acid sequences of the isozymes tested. On the other hand, we compared the amino acid sequences at the active site of the individual esterases and found that the sequences of all esterases tested are strictly conserved. These results strongly suggest that the esterases involved are classified into the serine hydrolase super family.

Amino Acid Sequence↗