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Showing papers on "Esterase published in 1969"



Journal ArticleDOI
TL;DR: C'1 esterase inhibitor has been found to block the actions of plasmin and the C'1r subcomponent of the first component of complement, and to retard the generation of PF/Dil.
Abstract: The fraction of human serum designated as C'1 esterase inhibitor is known to inhibit the action of C'1 esterase, a plasma kallikrein, and PF/Dil, an enzyme in plasma enhancing cutaneous vascular permeability. In the present study, C'1 esterase inhibitor has been found to block the actions of plasmin and the C'1r subcomponent of the first component of complement, and to retard the generation of PF/Dil. No inhibition of blood clotting or of the generation of plasmin was demonstrable.

302 citations


Journal ArticleDOI
TL;DR: The addition of Tween 80 and sucrose monopalmitate, nonionic surfactants, to fungal cultures resulted in marked increases in yields of the enzymes cellulase, amylase, sucrase, beta-1 --> 3 glucanase, xylanase, purine nucleosidase, and benzoyl esterase.
Abstract: The addition of Tween 80 and sucrose monopalmitate, nonionic surfactants, to fungal cultures resulted in marked increases in yields of the enzymes cellulase, amylase, sucrase, beta-1 --> 3 glucanase, xylanase, purine nucleosidase, and benzoyl esterase. The action appears to be an effect of the surfactant on cell permeability.

270 citations


Journal ArticleDOI
28 Feb 1969-Science
TL;DR: In the freshwater fish Catostomus clarkii, the frequency of alleles for polymorphic serum esterase varies with latitude, and coefficients of selection used to calculate allelic equilibrium within populations are derived from the activity profiles of the genotypes.
Abstract: In the freshwater fish Catostomus clarkii, the frequency of alleles for polymorphic serum esterase varies with latitude. The activity of the allele more frequent in southern populations increases as temperature increases from 0 ° to 37 °C, whereas activity of the allele more frequent in northern populations increases as temperature decreases. Coefficients of selection used to calculate allelic equilibrium within populations are derived from the activity profiles of the genotypes.

213 citations


Journal ArticleDOI
TL;DR: Esterase activity was present in all subcellular fractions but most enzyme activity was found in the 100,000 ×g defatted supernatant fraction, which produced no differences in esterase activity over saline-injected controls.
Abstract: Cholesterol esterase activity was measured in luteinized ovarian tissue from immature superovulated rats. Enzyme activity was determined from the rate of appearance of lmitic acid-l-14C, hydrolyzed from a cholesteryl pa lmitate-l-14C substrate during 30 min of incubation at 37 C. Direct proportionality of incubation time with hydrolysis and enzyme concentration with reaction velocity was established for the enzyme assay system. Esterase activity was present in all subcellular fractions but most enzyme activity was found in the 100,000 ×g defatted supernatant fraction. LH 10 ng), administered iv 1 hr before sacrifice, resulted in a highly significant (p <.001) increase esterase activity over saline-injected controls. suspension of 1500 ×g pellet from homogenized luteal tissue was incubated in the presence of ATP (1.7×10-3M), theophylline (10-3M) and LH or saline; the supernatant fractions from these incubations when added to the usual 100,000 ×g supernatant fraction produced no differences in esterase acti...

141 citations


Journal ArticleDOI
14 Feb 1969-Science
TL;DR: A comparison of highly purified C'1 esterase inhibitor from human serum and α2-neuraminoglycoprotein from human plasma by immunofusion, immuneelectrophoresis, and discgel electrophoresIS showed them to be antigenically identical.
Abstract: A comparison of highly purified C'1 esterase inhibitor from human serum and alpha(2)-neuraminoglycoprotein from human plasma by immunofusion, immuneelectrophoresis, and discgel electrophoresis showed them to be antigenically identical.

89 citations


01 Jan 1969
TL;DR: Evidence is presented in this paper that the kaolin-activated arginine esterase of plasma is related to plasma kallikrein activity and that it arises from a common precursor.
Abstract: A B S T R A C T Evidence is presented in this paper that the kaolin-activated arginine esterase of plasma is related to plasma kallikrein activity. Such a relationship is based on studies that (1) establish a constant ratio of esterase activity on various synthetic substrates for the kaolin-activated arginine esterase, purified kallikrein(s), and preparations obtained during the fractionation procedure; (2) exclude other known plasma and tissue arginine esterases; (3) confirm the requirement for factor XII in the activation of the enzyme precursor; and (4) show similarities in behavior between the plasma esterase and purified kallikrein (s) toward a variety of inhibitors. Based on this probable identification, evidence is provided that the concentration of active factor XII determines the rate of activation of plasma kallikreinogen, and that the activation may be blocked by polybrene. Once activated, plasma kallikrein is rapidly inactivated

84 citations


Journal ArticleDOI
TL;DR: In this article, it was shown that the concentration of active factor XII determines the rate of activation of plasma kallikreinogen, and that the activation may be blocked by polybrene.
Abstract: Evidence is presented in this paper that the kaolin-activated arginine esterase of plasma is related to plasma kallikrein activity Such a relationship is based on studies that (1) establish a constant ratio of esterase activity on various synthetic substrates for the kaolin-activated arginine esterase, purified kallikrein(s), and preparations obtained during the fractionation procedure; (2) exclude other known plasma and tissue arginine esterases; (3) confirm the requirement for factor XII in the activation of the enzyme precursor; and (4) show similarities in behavior between the plasma esterase and purified kallikrein(s) toward a variety of inhibitors Based on this probable identification, evidence is provided that the concentration of active factor XII determines the rate of activation of plasma kallikreinogen, and that the activation may be blocked by polybrene Once activated, plasma kallikrein is rapidly inactivated by the naturally occurring plasma inhibitor, but the inhibition is incomplete Acid or chloroform treatment of plasma rapidly inactivates the plasma inhibitor without affecting the concentration of plasma kallikreinogen Another plasma arginine esterase with properties suggestive of permeability factor is activated by factor XII in the presence of synthetic substrates, but only at low ionic strength The data suggest that this enzyme is closely related to plasma kallikrein and that it arises from a common precursor

84 citations



Journal ArticleDOI
TL;DR: The reaction of mercuripapain with glutaraldehyde resulted in an insoluble enzymes that possessed, after treatment with cysteine, approximately twice as much esterase and proteinase activities as did the insoluble enzyme prepared from papain.

69 citations



Journal ArticleDOI
TL;DR: Peptide mapping studies show that a single —SH group of transglutaminase previously identified as essential for all catalytic activities is not a component of the disulfide bridge formed as a result of DTNB treatment.

Journal ArticleDOI
TL;DR: A total of 541 strains belonging to 21 Oryza species were observed for leaf-blade isozymes of peroxidase and acid phosphatase, and 147 of them belonging to O. perennis and O. sativa for esterase isoz enzymes in addition, showing markedly differed in zymogram variability.
Abstract: A total of 541 strains belonging to 21 Oryza species were observed for leaf-blade isozymes of peroxidase and acid phosphatase, and 147 of them belonging to O. perennis and O. sativa for esterase isozymes in addition. The species markedly differed in zymogram variability. Widely distributed wild species generally had a large number of various zymograms, while localized wild species as well as cultivated ones showed limited variation. Though certain species had zymograms peculiar to them, identification of species by zymogram seemed to be difficult on account of wide variations within the species. The data were treated by the technique of pattern analysis to obtain an integrated picture. In the scatter diagrams obtained, closely related species were placed near one another but the distribution areas of their strains overlapped, suggesting that genes specifying the isozymes might be commonly distributed among different species. In both peroxidase and acid phosphatase, the cultivated species, sativa and glaberrima, had no zymograms of their own, as their zymograms, two for each, were present among those of their respective wild progenitors, Asian perennis and breviligulata. The two zymograms of sativa varieties represented the Indica and Japonica types, respectively. However, sativa varieties showed 19 different zymograms of esterase, the Indica and Japonica types differing in the frequencies of those peculiar to sativa.


Journal ArticleDOI
TL;DR: It is concluded that the integrity of hydrophobic interactions within the enzyme molecule is not equally critical with respect to the two activities and that it is possible to operate a change in enzyme specificity by a controlled change in hydrophilic interactions.


Journal ArticleDOI
TL;DR: The inhibitory profile of the activated phagocytic esterase was found to be essentially identical to the profile of inhibition previously obtained for the activated chemotactic ester enzyme of rabbit polymorphonuclear leukocytes, suggesting that the same enzyme may function in both chemotaxis andphagocytosis.
Abstract: The p-nitrophenyl ethyl phosphonate esters have been shown to inhibit complement-dependent erythrophagocytosis when exposed to guinea pig polymorphonuclear leukocytes prior to the initiation of phagocytosis. Inhibition of phagocytosis occurred in a manner characteristic of the well-defined capacity of phosphonate esters to inactivate serine esterases: inhibition was irreversible, dependent upon the temperature of reaction and pH of the reaction medium, and proportional to the concentration of inhibitor used and the duration of exposure between leukocytes and inhibitor. Phosphonate inhibition was further shown to be independent of any general cell damaging effects of the compounds used. The phagocytic enzyme inhibited by phosphonate esters apparently exists in or on leukocytes in an already activated state prior to the initiation of the phagocytic process. The inhibitory profile of the activated phagocytic esterase was found to be essentially identical to the profile of inhibition previously obtained for the activated chemotactic esterase of rabbit polymorphonuclear leukocytes, suggesting that the same enzyme may function in both chemotaxis and phagocytosis. Various substrates including acetate esters reported to protect the activated chemotactic esterase from inhibition by phosphonate esters did not exhibit a clear protective effect in the phagocytic system and attempts to define the relationship between the two enzymes were unsuccessful. Suggestive evidence was also obtained for the requirement of the function of a second, activatable esterase in the phagocytic process.

Journal ArticleDOI
TL;DR: Structures of special interest showing acetylesterase activity were: the growing hyphal tips of fungi, the vacuolated areas of yeast and protozoa, newly formed bacterial spores or immature fungal spores, "mesosome-like" bodies in Bacillus megaterium, and the cell membrane and nuclear region of green algae.
Abstract: The fluorogenic acetylesterase (acetic ester hydrolase EC 3.1.1.6.) substrate, fluorescein diacetate, was used to measure enzyme activity in living protist cells. The visual enzyme assay was done by monitoring fluorochromasia by fluorescent microscopy. Quantitative fluorogenic assays were done by measuring the evolved fluorescein in a fluorometer. Of 59 strains of bacteria, 35 were fluorochromatically positive. Eight of the fluorochromatically negative strains were fluorogenically positive. Of 22 strains of slime molds and fungi, all were fluorochromatically positive. Three out of 12 different algae were fluorochromatically positive. Several unidentified protozoa were also fluorochromatically positive. Four out of six protozoa were fluorochromatically positive. Structures of special interest showing acetylesterase activity were: the growing hyphal tips of fungi, the vacuolated areas of yeast and protozoa, newly formed bacterial spores or immature fungal spores, "mesosome-like" bodies in Bacillus megaterium, and the cell membrane and nuclear region of green algae. Yeast protoplasts and bacterial protoplasts and spheroplasts were fluorochromatically positive when derived from positive cells and negative when derived from negative cells. There was no correlation between the possession of a capsule and acetylesterase activity. There was no effect on the viability of bacterial cells incubated in the presence of fluorescein diacetate. Paraoxon inhibited bacterial and yeast enzyme at 10(-5)m. Eserine (10(-5)m) and Paraoxon (10(-7)m) inhibited B. megaterium enzyme. Sodium acetate at 10(-2)m did not inhibit bacterial enzyme. The implications of these findings on the location and expression of esterase activity in living cells are discussed.

Journal ArticleDOI
TL;DR: The enzyme hydrolyzes esters that are nonionic at a much greater rate than charged analogs and apparently an anionic charge on an ester inhibits the association between the esterase and ester.


Journal ArticleDOI
TL;DR: 2:3–Dichloro-1:4-naphthahydroquinone and several derivatives were prepared and tested in aqueous acetone solution against four fungi using a spore germination technique, and a relationship between ease of hydrolysis and fungicidal activity is apparent.
Abstract: 2:3–Dichloro-1:4-naphthahydroquinone and several derivatives were prepared and tested in aqueous acetone solution against four fungi using a spore germination technique. The hydroquinone showed the same order of fungicidal activity as 2:3-dichloro-1: 4-naphthaquinone, but was no less phytotoxic. Whilst the dibenzoyl ester and the dimethyl ether proved virtually inactive, the diacetyl ester was found to be as effective as 2:3-dichloro-1:4-naphthaquinone against Sclerotinia laxa, Botrytis fabae and Cladosporium fulvum, and also less phytotoxic to plum fruitlets and tomato and broad bean foliage. Reduced fungicidal activity was shown when the substance was formulated as an aqueous suspension suitable for field application. The rates of alkaline hydrolysis of these esters have been determined, and a relationship between ease of hydrolysis and fungicidal activity is apparent. It is suggested that these compounds, whilst not inherently active, are similarly hydrolysed to 2:3-dichloro-1:4-naphthahydroquinone in the presence of a fungal esterase. * Byrde, R. J. W., Crowdy, S. H. & Woodcock, D., ‘Studies on Systemic Fungicides. III’, Ann. appl. Biol. 40, 152, is regarded as Part I of this series.


Journal ArticleDOI
TL;DR: The findings indicate that gonadal effects on the hamster kidney may be of a more complex nature than has been considered heretofore and may be related to the estrogenic induction of renal adenocarcinoma, initiated under similar conditions, but not found with androgen-treated or other estrogenized animals.
Abstract: Thirteen esterase isozymes were separated from kidney extracts of normal adult Syrian hamsters (Mesocricetus auratus) using the zymogram technique with vertical starch gel electrophoresis and napht...


Journal ArticleDOI
TL;DR: Rat liver microsomal esterase has been purified 254-fold by a combination of solubilization in a mechanical cell homogenizer, acetone and ammonium sulfate precipitations, and hydroxylapatite column chromatography, and showed little hydrolytic activity on long chain mono-, and di- and triglycerides.

Journal ArticleDOI
TL;DR: The liver enzyme, located in the microsomal fraction, was solubilized by sonic disruption and purified 18-fold by diethylaminoethyl cellulose chromatography and Sephadex gel filtration, and the properties of carnitine ester hydrolase are discussed.

Journal Article
TL;DR: Active C′1s was isolated from the euglobulin fraction of human serum by column chromatography on CM and DEAE cellulose and Pevikon block electrophoresis and revealed a single precipitin line against horse anti-whole human serum on immunoelectrophoresIS and did not contain C′ 1q.
Abstract: Summary Active C′1s was isolated from the euglobulin fraction of human serum by column chromatography on CM and DEAE cellulose and Pevikon block electrophoresis. The final product revealed a single precipitin line against horse anti-whole human serum on immunoelectrophoresis and did not contain C′1q. A spectrophotometric assay was introduced for measuring the esterase activity of C′1s using TAMe as a substrate. Active C′1s was capable of generating SAC′4,2a although it did not bind to EAC′4 cells and EA. The esterase activity and the hemolytic activity as well as the C′2 and C′4 destructive activity of active C′1s were associated with a single homogeneous protein which migrated to the α-globulin region and had a molecular weight of approximately 110,000. A molecular titration of active C′1s is not possible because active C′1s transfers from site to site; however, SAC′4,2a generating activity could be correlated with TAMe esterase activity. As the ratio of hemolytic to esterase activity of active C′1s was 20 to 40 times less than that of C′1a, the firm binding of C′1a mediated through the combining site for antibody, presumably on the C′1q subunit, increases the efficiency of cleavage and transfer of C′2 at SAC′4.

Journal ArticleDOI
TL;DR: Electrophoretic studies of kidney homogenates of the house mouse have revealed two patterns in zone II of the esterase zymogram that are consistent with a two-allele, one-autosomal-locus mode of inheritance, with the allele for the absence of the multiple-band phenotype being dominant.
Abstract: Electrophoretic studies of kidney homogenates of the house mouse, Mus musculus, have revealed two patterns in zone II of the esterase zymogram. Animals of inbred strains C3H and C57BL/10 possess seven bands in this region and mice derived from a mating between a wild animal and a C3H mouse have only two bands of considerable activity in zone II. Breeding results are consistent with a two-allele, one-autosomal-locus mode of inheritance, with the allele for the absence of the multiple-band phenotype being dominant. Sensitivity data indicate that the esterases in zone II are aliesterases. Breeding and population data revealed that the zone II esterase-controlling locus is closely linked with but not identical to Es-1, Es-2 and Es-5 loci and so has been tentatively designated Es-6.


Journal ArticleDOI
TL;DR: It is tentatively concluded that esterase 1 of the rabbit peritoneal neutrophil is the activated form of the activatable esterases of chemotaxis, which after activation is capable of hydrolyzing aromatic amino acid esters and being inhibited by phosphonates.
Abstract: Previous published work has led to the hypothesis that the activatable esterase of chemotaxis is a serine esterase of the rabbit polymorphonuclear leukocyte existing in an inert, phosphonate insusceptible form, which after activation is capable of hydrolyzing aromatic amino acid esters and being inhibited by phosphonates In the present study, directed to the testing of this hypothesis, we have shown that rabbit peritoneal polymorphonuclear leukocytes contain three esterases capable of hydrolyzing the aromatic amino acid ester, acetyl DL-phenylalanine β-naphthyl ester Two of these esterases, esterase 1 and esterase 2, are inhibited by various p-nitrophenyl ethyl phosphonate esters The inhibition of each esterase is irreversible and progressive with time When the logarithm of the esterase activity remaining after cell and inhibitor have been in contact for a constant time is plotted against the concentration of inhibitor, a straight line results These results support the conclusion that both esterases are serine esterases The third esterase, esterase 3, differs from the other two by its inability to be inactivated by any of the phosphonates no matter how high the concentration of phosphonate or prolonged the period of incubation of cell with phosphonate The activity of esterase 1 is at least 10,000 times more easily inhibited by phosphonates than is that of esterase 2; incubating rabbit polymorphonuclear leukocytes for 15 min at 27°C with 10–9–10–8 M concentrations of various phosphonates inactivates esterase 1, but it required 10–6–10–4 M concentrations of the same phosphonates to inhibit esterase 2 The inhibition profiles of esterase 1 are distinctly different from those of esterase 2 when the two esterases are tested with the phenylalkylphosphonates, chloroalkylphosphonates, and alkylphosphonates The inhibition profile of esterase 1 is essentially the same as that of the activatable esterase of chemotaxis obtained previously when the same three homologous series of phosphonates were tested for their ability to protect against deactivation by the chemotactic factor or give chemotactic-dependent inhibition It is tentatively concluded that esterase 1 of the rabbit peritoneal neutrophil is the activated form of the activatable esterase of chemotaxis