Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ESTERASES”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 487 records · Page 27Linked to original sources
PubMedDate not supplied

Esterases in the malaria vector mosquito, Anopheles culicifacies. Genetic and linkage analyses of an alpha and beta polymorphism.

The genetic and linkage analyses of an alpha and beta esterase polymorphism in Anopheles culicifacies are presented. A survey of laboratory strains uncovered four electrophoretic variants for the alpha esterase and two for the beta esterase. Genetic analyses indicated that the variants of the alpha esterase are under the control of codominant alleles of a single locus and that this locus is linked to the locus controlling the expression of the codominant alleles of the beta esterases. The esterases are not linked either to sex (chromosome 1) or to maroon eye (chromosome 2) but to the chromosome 3 markers, dieldrin resistance and phosphoglucomutase. The gene sequence is Est-alpha--Dl--Pgm--Est-beta dnd the recombination frequencies are as follows: Est-alpha--Dl = 2.9 percent; Dl--Pgm = 5.8 percent; Pgm--Est-beta = 6.4 percent; Est-alpha--Est-beta = 15.1 percent, Est-alpha--Pgm = 8.7 percent and Dl--Est-beta = 12.2 percent.

Animals↗
PubMed1984

Distinctive electrophoretic and isoelectric focusing patterns of esterases from Yersinia enterocolitica and Yersinia pseudotuberculosis.

Esterases of 53 strains of Yersinia enterocolitica sensu stricto, including five previously defined biotypes, and 30 strains of Yersinia pseudotuberculosis were analysed by horizontal polyacrylamide-agarose gel electrophoresis and by isoelectrofocusing in thin-layer polyacrylamide gel. Esterase bands were defined by their range of activity towards several synthetic substrates, their resistance to heat and to di-isopropyl fluorophosphate. The two species were characterized by distinct electrophoretic patterns of their esterases. The apparent molecular weights of the heat-resistant esterase of Y. enterocolitica and of the major heat-resistant esterase of Y. pseudotuberculosis, as determined by polyacrylamide gradient gel electrophoresis, were estimated to be 52 000 and 250 000, respectively. On the basis of electrophoretic mobilities and isoelectric points of esterases produced by strains of Y. enterocolitica, five principal zymotypes were observed: two for strains of biotype 1, two for strains of biotypes 2 and 3, respectively, and only one for strains of both biotypes 4 and 5. The zymotypes of strains of biotypes 2, 3, 4 and 5 appeared to be more closely related to one another than to zymotypes of strains of biotype 1. Variations in number or mobility of bands observed within each biotype of Y. enterocolitica and within some serotypes of Y. pseudotuberculosis could represent an additional marker for epidemiological analysis.

Electrophoresis, Polyacrylamide Gel↗
PubMed1994

Genetic heterogeneity of Pseudomonas aeruginosa clinical isolates revealed by esterase electrophoretic polymorphism and restriction fragment length polymorphism of the ribosomal RNA gene region.

The intra-species differentiation of Pseudomonas aeruginosa was analysed by comparing the polymorphism of esterases by conventional polyacrylamide-agarose gel electrophoresis, the physicochemical properties of the variants of the major esterase P3 and the restriction fragment length polymorphism of ribosomal RNA gene regions (ribotyping) to O-serotyping for several panels of strains selected from among a series of 257 clinical isolates and two references strains, (ATCC nos. 10145 and 27853). The electrophoretic variation of four main kinds of esterase (P1-P4) and 11 additional esterases distinguished by their spectra of hydrolytic activity with synthetic substrates and by their sensitivity to di-isopropylfluorophosphate, allowed the discrimination of 67 zymotypes. Thirty-two esterase P3 variants were characterized by their pI, electrophoretic mobilities and titration curve analyses. They were distributed into two groups which, by these molecular criteria, seem to be distantly related. Combination of the patterns resulting from HindIII, EcoRI and BclI restriction endonuclease digestions allowed the discrimination of 33 ribotypes among 134 strains. The strains exhibiting esterase P3 variants of group 2 presented a distinct ribotype and belonged to serotype (O)12. They could constitute a distinct group within the species. For the majority of the strains, the absence of correlation between zymotype, ribotype and serotype argues for a high level of heterogeneity within P. aeruginosa and indicates that the parallel use of the first two methods represent a potential tool for epidemiological study.

DNA, Ribosomal↗
PubMed2002

EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity.

Esterases form a diverse class of enzymes of largely unknown physiological role. Because many drugs and pesticides carry ester functions, the hydrolysis of such compounds forms at least one potential biological function. Carboxylesterases catalyze the hydrolysis of short chain aliphatic and aromatic carboxylic ester compounds. Esterases, D-alanyl-D-alanine-peptidases (DD-peptidases) and beta-lactamases can be grouped into two distinct classes of hydrolases with different folds and topologically unrelated catalytic residues, the one class comprising of esterases, the other one of beta-lactamases and DD-peptidases. The chemical reactivities of esters and beta-lactams towards hydrolysis are quite similar, which raises the question of which factors prevent esterases from displaying beta-lactamase activity and vice versa. Here we describe the crystal structure of EstB, an esterase isolated from Burkholderia gladioli. It shows the protein to belong to a novel class of esterases with homology to Penicillin binding proteins, notably DD-peptidase and class C beta-lactamases. Site-directed mutagenesis and the crystal structure of the complex with diisopropyl-fluorophosphate suggest Ser75 within the "beta-lactamase" Ser-x-x-Lys motif to act as catalytic nucleophile. Despite its structural homology to beta-lactamases, EstB shows no beta-lactamase activity. Although the nature and arrangement of active-site residues is very similar between EstB and homologous beta-lactamases, there are considerable differences in the shape of the active site tunnel. Modeling studies suggest steric factors to account for the enzyme's selectivity for ester hydrolysis versus beta-lactam cleavage.

Amino Acid Sequence↗
PubMed1986

Biosynthesis of rat-liver pI-5.0 esterases in cell-free systems and in cultured hepatocytes.

Rat liver esterases focusing at pH 5.0 (referred to below as pI-5.0 esterases) are structurally related glycoproteins which differ slightly in their mobility in sodium dodecyl sulphate/polyacrylamide gel electrophoresis (SDS-PAGE). They reside in the lumen of the endoplasmic reticulum. We have studied their biosynthesis in cell-free systems programmed by total liver RNA, using sheep and rabbit antibodies to isolate the translation products related to these enzymes. Our results show that they are assembled as a precursor polypeptide chain (62 kDa) larger than the mature proteins. The pI-5.0 esterase mRNA could be extracted from bound but not free polysomes. Reticulocyte lysates supplemented with dog pancreas microsomes produced four esterase-related components in segregated form (61, 60, 58 and 56 kDa). The largest three correspond in electrophoretic mobility to the mature enzymes. They are glycoproteins that bind to concanavalin A, and can be reduced to the size of the shortest component by endo-beta-N-acetylglucosaminidase H (endo-H). Immunoprecipitation after biosynthetic labeling of the proteins in cultured hepatocytes also gave three glycosylated components that had the same mobility in SDS-PAGE as the mature enzymes. When tunicamycin was present in the culture medium, a single immunoprecipitable form was observed. Its apparent Mr was similar to that of the unglycosylated pI 5.0 esterase form synthesized in vitro in the presence of dog pancreas microsomes. Thus the biosynthesis of these esterases has characteristics in common with that of numerous secretory proteins, except for the rather large difference in size (approximately equal to 6 kDa) resulting from the proteolytic processing of their in-vitro-synthesized precursor.

Acetylglucosaminidase↗
PubMed2006

A novel phenotype based on esterase electrophoretic polymorphism for the differentiation of Lactococcus lactis ssp. lactis and cremoris.

AIMS: To evaluate the esterase phenotype in Lactococcus lactis strains isolated from traditional Tunisian dairy products. METHODS AND RESULTS: A collection of 55 L. lactis strains isolated from traditional fermented milk products and three reference strains were identified at species and subspecies level using molecular methods targeted to the 16S rRNA gene and to the histidine operon. The genotypic data obtained allowed the identification of the strains as L. lactis ssp. lactis and L. lactis ssp. cremoris with the prevalence of the ssp. lactis. The phenotypic identification based on arginine hydrolysis, the growth at 40 degrees C and in presence of 4% NaCl showed several discrepancy with the identification data based on genotypic analysis. Additional experiments carried out evaluating the esterase electrophoretic patterns revealed four classes of esterases identified on the basis of their electrophoretic mobility and specific activity on alpha- and beta-naphthyl ester of acetate and propionate. Esterase profiles discriminated the strains in two main groups corresponding to the subspecies cremoris and lactis according to a DNA-based identification. CONCLUSIONS: The evaluation of esterase activity represents a novel phenotype for the taxonomic discrimination of the L. lactis ssp. lactis and cremoris. SIGNIFICANCE AND IMPACT OF THE STUDY: Besides the DNA-based techniques that allow the rapid and accurate species/subspecies identification, the electrophoretic esterase profiles of L. lactis strains represents: (i) a new phenotypic tool to understand the physiology and the ecology of this species; and (ii) a new test for the potential selection of flavour producing strains.

Esterases↗
PubMed1984

Release of kallikrein-like esterase and tonin from dispersed cells of the rat submandibular gland.

Viable dispersed cell preparations of rat submandibular gland were obtained by a tissue-dissociation procedure using collagenase and gentle mechanical force. The cells released kallikrein-like esterase in a time- and calcium-dependent manner in response to noradrenaline (10 microM) at 30 degrees C. The net loss of kallikrein-like esterase content from the dispersed cells corresponded with the increase in kallikrein-like esterase activity in the suspending medium at all concentrations of noradrenaline. These results indicate the viability and functional integrity of this dispersed cell preparation of rat submandibular gland. alpha-Adrenoceptor agonists such as noradrenaline stimulated kallikrein-like esterase and tonin release in a dose-dependent manner, whereas the beta-adrenoceptor agonist isoprenaline and cholinoceptor agonist methacoline were both inactive. Noradrenaline-induced release of kallikrein-like esterase and tonin were completely blocked by prior addition of the alpha-adrenoceptor antagonist, phenoxybenzamine. It is concluded that the secretion of kallikrein-like esterase and tonin in rat submandibular gland is mediated only via stimulation of alpha-adrenoceptors.

Adrenergic alpha-Agonists↗
PubMed2006

Effect of cytochromes P450 chemical inhibitors and monoclonal antibodies on human liver microsomal esterase activity.

Selective and nonselective cytochromes P450 (P450) chemical inhibitors and monoclonal antibodies (mAbs) are routinely used to determine the contribution of P450 enzymes involved in the biotransformation of a drug. A fluorometric assay has been established using fluorescein diacetate as a model substrate to determine the effect of some commonly used P450 inhibitors and mAbs on human liver microsomal esterase activity. Of those inhibitors studied, only alpha-naphthoflavone, clotrimazole, ketoconazole, miconazole, nicardipine, and verapamil significantly inhibited human liver microsomal esterase activity, with apparent IC50 values of 18.0, 20.5, 6.5, 15.0, 19.4, and 5.4 microM, respectively. All of these showed > or =20% inhibition of human liver microsomal esterase activity at concentrations typically used for P450 reaction phenotyping studies, with clotrimazole, miconazole, nicardipine, and verapamil showing >60% inhibition. Unlike the chemical inhibitors, no inhibition of human liver microsomal esterase activity was observed in the presence of mAb to CYP1A2, 2C8, 2C9, 2C19, 2D6, and 3A4. These results suggest that P450 chemical inhibitors are capable of inhibiting human liver microsomal esterase activity and should not be used to assess the role of P450 enzymes in the biotransformation of esters. The lack of inhibition of human liver microsomal esterase activity by P450-specific monoclonal antibodies suggests that they may be used to assess the role of P450 enzymes in the biotransformation of esters. Additional experiments to assess the contribution of oxidative enzymes in the metabolism of esters may include incubations in the presence and absence of beta-nicotinamide adenine dinucleotide 2'-phosphate reduced.

Antibodies, Monoclonal↗
PubMed2000

Cloning, characterization, controlled overexpression, and inactivation of the major tributyrin esterase gene of Lactococcus lactis.

The gene encoding the major intracellular tributyrin esterase of Lactococcus lactis was cloned using degenerate DNA probes based on 19 known N-terminal amino acid residues of the purified enzyme. The gene, named estA, was sequenced and found to encode a protein of 258 amino acid residues. The transcription start site was mapped 233 nucleotides upstream of the start codon, and a canonical promoter sequence was identified. The deduced amino acid sequence of the estA product contained the typical GXSXG motif found in most lipases and esterases. The protein was overproduced up to 170-fold in L. lactis by use of the nisin-controlled expression system recently developed for lactic acid bacteria. The estA gene was inactivated by chromosomal integration of a temperature-sensitive integration vector. This resulted in the complete loss of esterase activity, which could then be recovered after complementation of the constructed esterase-deficient strain with the wild-type estA gene. This confirms that EstA is the main enzyme responsible for esterase activity in L. lactis. Purified recombinant enzyme showed a preference for short-chain acyl esters, surprisingly also including phospholipids. Medium- and long-acyl-chain lipids were also hydrolyzed, albeit less efficiently. Intermediate characteristics between esterases and lipases make intracellular lactococcal EstA difficult to classify in either of these two groups of esterolytic enzymes. We suggest that, in vivo, EstA could be involved in (phospho)lipid metabolism or cellular detoxification or both, as its sequence showed significant similarity to S-formylglutathione hydrolase (FGH) of Paracoccus denitrificans and human EstD (or FGH), which are part of a universal formaldehyde detoxification pathway.

Amino Acid Sequence↗
PubMed2002

Decreasing the level of ethyl acetate in ethanolic fermentation broths of Escherichia coli KO11 by expression of Pseudomonas putida estZ esterase.

During the fermentation of sugars to ethanol relatively high levels of an undesirable coproduct, ethyl acetate, are also produced. With ethanologenic Escherichia coli strain KO11 as the biocatalyst, the level of ethyl acetate in beer containing 4.8% ethanol was 192 mg liter(-1). Although the E. coli genome encodes several proteins with esterase activity, neither wild-type strains nor KO11 contained significant ethyl acetate esterase activity. A simple method was developed to rapidly screen bacterial colonies for the presence of esterases which hydrolyze ethyl acetate based on pH change. This method allowed identification of Pseudomonas putida NRRL B-18435 as a source of this activity and the cloning of a new esterase gene, estZ. Recombinant EstZ esterase was purified to near homogeneity and characterized. It belongs to family IV of lipolytic enzymes and contains the conserved catalytic triad of serine, aspartic acid, and histidine. As expected, this serine esterase was inhibited by phenylmethylsulfonyl fluoride and the histidine reagent diethylpyrocarbonate. The native and subunit molecular weights of the recombinant protein were 36,000, indicating that the enzyme exists as a monomer. By using alpha-naphthyl acetate as a model substrate, optimal activity was observed at pH 7.5 and 40 degrees C. The Km and Vmax for alpha-naphthyl acetate were 18 microM and 48.1 micromol. min(-1). mg of protein(-1), respectively. Among the aliphatic esters tested, the highest activity was obtained with propyl acetate (96 micromol. min(-1). mg of protein(-1)), followed by ethyl acetate (66 micromol. min(-1). mg of protein(-1)). Expression of estZ in E. coli KO11 reduced the concentration of ethyl acetate in fermentation broth (4.8% ethanol) to less than 20 mg liter(-1).

Acetates↗
PubMed1996

Induction of an extracellular esterase from Candida albicans and some of its properties.

An extracellular esterase from Candida albicans A-714 was found to be induced in a medium containing 0.7% yeast nitrogen base and 2.5% Tween 80 (polyoxyethylenesorbitan compounds). Enzyme activity, which exists predominantly in the extracellular space, was measured by a colorimetric method using alpha-naphthyl palmitate as a substrate. The induction level of the esterase activity was found to be well correlated with fungal growth and was dependent on the Tween 80 concentration. Such esterase activity was observed only in medium containing Tween 80 or other Tweens as the sole carbon source and therefore was not observed in either peptone-glucose medium or peptone-glucose medium supplemented with Tween 80. The induced esterase was heat labile and had maximum activity at pH 5.5. Enzyme activity was stimulated by the addition of sodium taurocholate, an activator of lipase. Thin-layer chromatography revealed that this enzyme does not hydrolyze triolein and L-alpha-lecithin, suggesting that it is a monoester hydrolase (not a lipase in the strict sense of the word). Esterase activity was examined in 85 clinical isolates of Candida species; C. albicans, C. tropicalis, and C. parapsilosis tended to have higher enzyme activities than C. kefyr, C. krusei, C. glabrata, and C. guilliermondii. Although the physiological properties of this esterase are not clear at present, it was found to be crucial for fungal growth under specific conditions.

Candida albicans↗
PubMed1987

Purification and characterization of a novel extracellular esterase from pathogenic Streptomyces scabies that is inducible by zinc.

Native polyacrylamide gels of extracellular proteins produced by several Streptomyces isolates grown with suberin were assayed in situ for esterase activity. Two pathogenic isolates of Streptomyces scabies from different geographical regions were found to produce a similar esterase activity that was not produced by nonpathogenic strains. After treatment with EDTA, suberin no longer induced esterase production. Expression was restored when EDTA-treated suberin was supplemented with zinc. The optimal concentration of zinc required for esterase production was 2 microM. This esterase was purified from one of the pathogenic isolates and characterized. The enzyme was 38,000 daltons when determined by gel filtration on Sephadex G-100 and 36,000 daltons when determined by denaturing polyacrylamide gel electrophoresis. The esterase showed maximal activity in sodium phosphate buffer above pH 8.0, was stable to temperatures of up to 60 degrees C, and had an apparent Km of 125 microM p-nitrophenyl butyrate.

Enzyme Induction↗
PubMed1992

Identification of a cocaine esterase in a strain of Pseudomonas maltophilia.

A strain of Pseudomonas maltophilia (termed MB11L) which was capable of using cocaine as its sole carbon and energy source was isolated by selective enrichment. An inducible esterase catalyzing the hydrolysis of cocaine to ecgonine methyl ester and benzoic acid was identified and purified 22-fold. In the presence of the solubilizing agent cholate, cocaine esterase had a native Mr of 110,000 and was shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be a monomer. In the absence of cholate, cocaine esterase had a native Mr of 410,000 and probably existed as a tetramer. The pH optimum of the enzyme was 8.0, and the Km values for cocaine, ethyl benzoate, and ethyl 2-hydroxybenzoate were 0.36, 1.89, and 1.75 mM, respectively. Inhibition studies indicated that the enzyme was a serine esterase, possibly possessing a cation-binding site similar to those of mammalian acetylcholinesterase and the atropine esterase of Pseudomonas putida PMBL-1. The cocaine esterase of P. maltophilia MB11L showed no activity with atropine, despite the structural similarity of cocaine and atropine.

Benzoates↗
PubMed1987

Leucocyte esterase test as rapid screen for non-gonococcal urethritis.

The two standard tests for the initial diagnosis of non-gonococcal urethritis (NGU), microscopic examination of gram stained urethral smears and the two glass urine test, have the disadvantage of being insensitive and subjective. The leucocyte esterase test detects enzymes specific to polymorphonuclear leucocytes and can therefore be used as a sensitive indicator of pyuria. This study sought to evaluate its use as a rapid, sensitive, and non-subjective method of screening for NGU. Of the 81 men with urethral symptoms in the study group, 26 had more than 5 polymorphonuclear leucocytes per high power field (x 1000) and all 26 were leucocyte esterase test positive; whereas 55 had fewer than 5 polymorphonuclear leucocytes per high power field, but 29 (53%) of them had a positive leucocyte esterase test result. In addition, 25 patients in the study group yielded Chlamydia trachomatis on culture. Of these 25, 24 (96%) were leucocyte esterase test positive, whereas only 11 (44%) were Gram stain positive. All 40 patients in the control group (without urethral symptoms or signs) were leucocyte esterase test negative. The leucocyte esterase test is thus a rapid, sensitive, and non-subjective screening aid in the diagnosis of NGU.

Adolescent↗
PubMed1996

Dietary induction of pancreatic cholesterol esterase: a regulatory cycle for the intestinal absorption of cholesterol.

Atherosclerosis has a strong dietary basis without a proven molecular mechanism for cholesterol absorption. To investigate the potential role of pancreas in this process and its interaction with the two dietary forms of cholesterol (free and esterified), we undertook to study the role of pancreatic cholesterol esterase in cholesterol absorption. The results showed that (i) cholesterol esters contribute a disproportionately high fraction of absorbed dietary cholesterol, (ii) rates of intestinal cholesterol absorption are related to pancreatic cholesterol esterase activity, (iii) mRNA specific for pancreatic cholesterol esterase is induced 15-fold by dietary sterol esters and 10-fold by free sterol, (iv) the induction of cholesterol esterase mRNA is reversible, and (v) free cholesterol transport into cultured human intestinal cells is enhanced 300% by pancreatic cholesterol esterase. These data implicate pancreatic cholesterol esterase as pivotal in a metabolic loop under positive feedback control for the absorption of dietary cholesterol, whether free or esterified.

Adenocarcinoma↗
PubMed1977

Origin of esterases in human whole saliva.

Whole saliva of 59 healthy persons was used for determination of esterase activity. The pattern of esterase was studied by means of isoelectrofocusing on thin-layer acrylamide gels. The esterases found in whole saliva are suggested to be derived from the cells of the tissue in the oral cavity. This origin is indicated (e.g.) by comparison between isolectrophoretic esterase patterns of whole saliva, submandibular saliva, gingival biopsy and fibroblast culture. Antisera against partially purified saliva esterases were produced in rabbits. These sera, used in immunoelectro-osmophoresis, gave esterase-active immunoprecipitate against whole saliva, the water-soluble materials of disrupted gingival biopsy and fibroblast culture, but not against the material of the bacteria, Streptococcus sanguis, Strptococcus mutans, Streptococcus mitis, Actinomyces viscosus and Lactobacillus fermentum.

Amylases↗
PubMed1969

Studies on the prekallikrein (kallikreinogen)--kallikrein enzyme system of human plasma. II. Evidence relating the kaolin-activated arginine esterase to plasma kallikrein.

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.

Aprotinin↗
PubMed1987

Ultrastructural cytochemical and autoradiographic demonstration of nonspecific esterase(s) in guinea pig basophils.

We used ultrastructural autoradiographic and cytochemical methods to localize esterase activities in unstimulated guinea pig basophils and in basophils undergoing degranulation or recovery from degranulation. We used tritium-labeled diisopropylfluorophosphate (DFP) as a probe for serine enzymes and localized this probe by ultrastructural autoradiography to cytoplasmic granules of immature or mature unstimulated basophils, as well as to granules released by degranulating basophils. Ultrastructural cytochemistry using alpha naphthyl acetate (ANA) as substrate localized nonspecific esterase activity to extruded granules, either within the interiors of degranulation sacs or within granules completely separated from degranulating basophils. Extruded granules retained their esterase activity for as long as 24 hr after antigen-induced degranulation. The plasma membranes of unstimulated or degranulating basophils, as well as of basophils recovering from degranulation, displayed prominent cell surface ANA esterase ectoenzyme activity. Lipid bodies, organelles present in the cytoplasm of both control and recovering basophils, were also alpha naphthyl acetate esterase (ANAE)-positive. Thus, cytochemical and autoradiographic techniques localized esterase and/or [3H]-DFP-binding activities to cytoplasmic granules, lipid bodies, and cell surface of basophils, and these enzyme activities persisted during both degranulation and recovery from degranulation.

Animals↗