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PubMed1983

Presumptive screening test for seminal acid phosphatase using sodium thymolphthalein monophosphate.

The use of sodium thymolphthalein monophosphate for presumptive seminal acid phosphatase testing is discussed. Recent evidence reveals that the dye (o-dianisidine) used in conjunction with alpha-naphthyl phosphate for seminal acid phosphatase testing is a carcinogenic hazard. Numerous tests for seminal acid phosphatase were conducted with swabs from sexual assault kits to compare both substrates. Results of tests using sodium thymolphthalein or alpha-naphthyl phosphate correlated exactly. Sodium thymolphthalein is an effective alternative for preliminary seminal fluid analysis because of its high degree of selectivity and stability, and because it eliminates the potential health hazard.

Acid Phosphatase↗
PubMed1983

RNA and homology mapping of two DNA fragments with repressible acid phosphatase genes from Saccharomyces cerevisiae.

Two EcoRI restriction fragments carrying Saccharomyces cerevisiae repressible acid phosphatase genes were analyzed. Transcripts were mapped by restriction endonuclease cleavage of glyoxal-stabilized R-loops and by gel blot hybridizations to cDNA. Homology between the two fragments was examined by gel blots and heteroduplex analysis. Each fragment carried a region of about 1.5 kilobases that coded for a repressible acid phosphatase, and these regions showed homology to one another. In addition, one fragment carried a second region of somewhat lower homology that probably codes for the so-called constitutive acid phosphatase.

Acid Phosphatase↗
PubMed1979

Human prostatic acid phosphatases: purification of a minor enzyme and comparisons of the enzymes.

The minor enzyme of human prostatic acid phosphatases (pI 5.5) with high specific activity (orthophosphoric monoester phosphohydrolase, acid optimum, EC 3.1.3.2) has been purified for the first time as a pure enzyme protein. The enzyme was a single protein when examined by polyacrylamide gel electrophoresis and isotachophoresis. The specific activity was 1080 micromole per (min X mg) for hydrolysis of 5.5 mmole per liter of p-nitrophenylphosphate at pH 4.8 and 37 C. The purification coefficient was 540 and the recovery of enzyme activity was 2 per cent. The molecular weight of the enzyme subunit when measured by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate was 54,000. The Km of the purified enzyme was 3 X 10(-4) mole per liter for p-nitrophenylphosphate. An antiserum to this enzyme was prepared. The enzyme was cross-reactive with the main enzyme (pI 4.9) of human prostatic acid phosphatases in immunoelectrophoresis. No precipitin arc with the acid phosphatase in the serum of a prostatic carcinoma patient could be shown. Antiserum to the main enzyme caused a precipitin line with the same serum sample.

Acid Phosphatase↗
PubMed1976

Improved determination of prostatic acid phosphatase (sodium thymolphthalein monophosphate substrate).

We have modified a previously described method for determining acid phosphatase, with thymolphthalein monophosphate as substrate, to increase its sensitivity. We assessed effects of serum on variables influencing acid phosphatase activity as measured by this method. The method is shown to be not completely specific for prostatic acid phosphatase. The importance of standardizing methodology in measurement of enzyme activities is demonstrated.

Acid Phosphatase↗
PubMed1991

[Localization of acid phosphatase in Saccharomyces cerevisiae and its export into culture media depends on the type of the N-terminal signal peptide].

The aim of this work was to study the character of intracellular distribution and efficiency of yeast acid phosphatase export depending on the type of the N-terminal signal peptide used. A number of plasmids carrying the acid phosphatase genes with different signal peptides sequences was constructed. The main site of the enzyme accumulation for the variant containing its own acid phosphatase signal peptide was the periplasm. Approximately the same pattern was observed when the hybrid signal peptide consisting of acid phosphatase signal peptide and alpha-factor preprosegment tandem was used. Unlike the above-mentioned systems the strain carrying acid phosphatase under the control of alpha factor preprosegment was able to export the enzyme into the culture medium. The experiments have shown the possibility of changing the final localization of secretory proteins by replacing the N-terminal signal peptide.

Acid Phosphatase↗
PubMed1992

Circulating levels of tartrate-resistant acid phosphatase in macrophage-activated lung disease.

Tartrate-resistant acid phosphatase (TrACP) is abundant in alveolar macrophages, suggesting that these cells might contribute to the activity of this isoenzyme in sera of patients with conditions characterized by activation of alveolar macrophages. TrACP was therefore measured in patients with pulmonary sarcoidosis and cryptogenic fibrosing alveolitis and compared with values in controls. Since osteoclasts are known to be the main source of TrACP in serum several indices of bone-turnover were also measured: serum bone-specific alkaline phosphatase and urine hydroxyproline:creatinine ratios. Patients with Paget's disease of bone constituted a reference group presenting increased bone turnover. TrACP was not significantly higher in the lung-disease groups than in controls, although there was a strong positive correlation with angiotensin-converting enzyme in pulmonary sarcoidosis. As expected, TrACP activity was elevated together with the other indices of bone turnover in Paget's disease. It is unlikely that TrACP from alveolar macrophages contributes significantly to serum acid phosphatase activity in lung disease.

Acid Phosphatase↗
PubMed1985

The presence of essential histidine residues in manganese(III)-containing acid phosphatase from sweet potato.

Chemical modification studies of manganese(III)-containing acid phosphatase [EC 3.1.3.2] were carried out to investigate the contributions of specific amino-acid side-chains to the catalytic activity. Incubation of the enzyme with N-ethylmaleimide at pH 7.0 caused a significant loss of the enzyme activity. The inactivation followed pseudo-first-order kinetics. Double log plots of pseudo-first-order rate constant vs. concentration gave a straight line with a slope of 1.02, suggesting that the reaction of one molecule of reagent per active site is associated with activity loss. The enzyme was protected from inactivation by the presence of molybdate or phosphate ions. Amino acid analyses of the N-ethylmaleimide-modified enzyme showed that the 96%-inactivated enzyme had lost about one histidine and one-half lysine residue per enzyme subunit without any significant decrease in other amino acids, and also demonstrated that loss of catalytic activity occurred in parallel with the loss of histidine residue rather than that of lysine residue. Molybdate ions also protected the enzyme against modification of the histidine residue. The enzyme was inactivated by photooxidation mediated by methylene blue according to pseudo-first-order kinetics. The pH profile of the inactivation rates of the enzyme showed that an amino acid residue having a pKa value of approximately 7.2 was involved in the inactivation. These studies indicate that at least one histidine residue per enzyme subunit participates in the catalytic function of Mn(III)-acid phosphatase.

Acid Phosphatase↗
PubMedDate not supplied

Acid phosphatase of the rat epididymis. III. Histochemical and biochemical responses in experimental conditions.

The specific activities of three acid phosphatases were followed in the epididymis of growing rats. All activities were constantly rising but revealed two steeper parts probably corresponding to the increase of androgen secretion and the arrival of spermatozoa in the epididymis. Simultaneously an increase in the histochemical staining was obtained in all epididymal segments. Both biochemical and histochemical studies showed that castration reduced the activity of all acid phosphatases and this could be restored with testosterone-estradiol treatment. Estradiol had no effect on the activities in the castrated animal, but in the normal animal it caused an elevation of Enzyme I activity. In the histochemical study estradiol seemed to restore the acid phosphatase activity. Enzyme I reacted slower than the others to both castration and hormone treatment. Increased elimination caused by ligation of the epididymis caused a reduction in the activity of all enzymes within four days. It was greatest in the area of the corpus. This study, however, rendered no further elucidation for the assumption that acid phosphatases participate in the elimination of excessive and defective spermatozoa.

Acid Phosphatase↗
PubMed1983

Glycoprotein exhibiting immunological and enzymatic activities of human prostatic acid phosphatase.

A glycoprotein (GP) which is immunochemically and biologically related to human prostatic acid phosphatase (PAP) has been isolated from human seminal plasma by ammonium sulfate precipitation followed by sequential concanavalin A:Sepharose 4B column, anion-exchange chromatography and gel filtration. The purified GP was shown to be homogeneous by disc- and sodium dodecyl sulfate: polyacrylamide gel electrophoresis. The apparent molecular weight of purified GP was estimated to be 50,000 by gel filtration and 45,000 by sodium dodecyl sulfate: gel electrophoresis. In gel diffusion against antiserum to purified PAP, a partial immunological identity was shown between GP and PAP. This was further confirmed by an inhibition reaction between GP and antiserum to purified GP by PAP. Significantly, 30% of PAP enzyme activity was inhibited by anti-GP antiserum, while only 5% was inhibited by anti-PAP antiserum. Purified GP was shown to exhibit a weak, but significant, acid phosphatase activity by hydrolyzing alpha-naphthyl phosphate at pH 5.6. The Km and Vmax for GP are 1.6 X 10(-4) M and 0.056 mumol/min/microgram protein, respectively, using alpha-naphthyl phosphate as the substrate. In the presence of anti-PAP antibody, the enzyme activity of GP was enhanced severalfold. Furthermore, the acid phosphatase activity of GP also was inhibited by tartrate, which is the most commonly used inhibitor for PAP. GP and PAP were found to have different carbohydrate content, amino acid composition, amino-terminal sequence, and peptide map. Thus, GP represents a newly identified protein. The significance of these results at molecular and clinical levels is discussed.

Acid Phosphatase↗
PubMed1993

Monoclonal antibodies directed against Leishmania secreted acid phosphatase and lipophosphoglycan. Partial characterization of private and public epitopes.

Leishmania promastigotes, the stage of the parasite characteristic for the sandfly vector, express an abundant glycoconjugate, called lipophosphoglycan, at their surface. Lipophosphoglycan consists of lysoalkyl-sn-glycerophosphoinositol linked to a phosphosaccharide core conserved in all species, which is connected to PO4-6Gal beta 1,4Man alpha 1 repeats with species-specific substitutions at the Gal residue; the repeats are capped by conserved and species-specific oligosaccharides. Most Leishmania species also secrete an acid phosphatase, which, in Leishmania mexicana, is a filamentous complex composed of a phosphorylated glycoprotein and non-covalently associated proteo-(high-molecular-mass)phosphoglycan. The secreted acid phosphatase complex was used as an antigen to derive a panel of monoclonal antibodies (mAbs). A total of 25 mAbs (17 novel and 8 previously described) were tested by different techniques for their specificity against lipophosphoglycan and secreted acid phosphatase from several Leishmania species. This comparison and the modification of the antigens by chemical or enzymic treatments allowed a classification of the mAbs into several groups. First, from 25 mAbs examined, 22 recognize lipophosphoglycan and the enzyme complex of L. mexicana; only three are specific for secreted acid phosphatase. Two of the latter group are also directed against carbohydrate structures, whereas the third mAb recognizes the 100-kDa polypeptide of the complex. The secreted acid-phosphatase-specific class detects antigen in the flagellar pocket of promastigotes while all anti-lipophosphoglycan mAbs bind to the cell surface. Second, all 15 anti-lipophosphoglycan mAbs investigated in detail appear to be directed against the phosphosaccharide repeats or the cap structure rather than the phosphosaccharide core. Two mAbs recognize terminal cap-structures containing Man alpha 1,2Man residues. Four antibodies are specific for L. mexicana and are probably directed against PO4-6[Glc beta 1,3]Gal beta 1,4Man alpha 1 repeats while six mAbs react with the unmodified repeats. Two antibodies specific for Leishmania major recognize Gal beta 1,3-substituted repeats unique for lipophosphoglycan from this species. Analysis by immunoblotting indicates that the high-molecular-mass proteo-phosphoglycan of L. mexicana secreted acid phosphatase carries epitopes for all anti-lipophosphoglycan mAbs suggesting the presence of capped phosphosaccharide repeats while the enzymically active glycoprotein subunit is modified by caps but probably not by repeats. In the case of Leishmania donovani secreted acid phosphatase, the enzymically active polypeptide may be directly modified by repeats. The mAbs are used to characterize changes in lipophosphoglycan structure, which occur in culture during the transition of promastigotes from the logarithmic to the stationary growth phase.(ABSTRACT TRUNCATED AT 400 WORDS)

Acid Phosphatase↗
PubMed1982

Chronological changes in acid phosphatase activity within neurons and perineuronal satellite cells of the inferior vagal ganglion of the cat induced by vagotomy.

The hexazonium pararosaniline method was employed to describe the distribution of acid phosphatase activity, chronologically, within neurons and their investing satellite cells of the inferior vagal ganglion of the cat after vagotomy. In control ganglia, acid phosphatase activity was invariably confined to the cytoplasm of neurons and satellite cells. Reaction product was visible as distinct granules within neuronal perikarya. The cytoplasm of perineuronal satellite cells also contained reaction product but, in most instances, activity was weak and granules were difficult to distinguish. No reaction product was observed in myelin or axonal processes; nuclear staining was absent. Acid phosphatase activity was increased in ganglionic neurons as early as 24 hours after vagotomy. Increased activity in perineuronal satellite cells was not evident until 3 days post-operatively. By 15 days, activity was ubiquitously increased in the cytoplasm of both neurons and satellite cells. Evidence suggesting neuronophagia was also apparent. Between 30 and 60 days post-operatively acid phosphatase activity gradually decreased in both neurons and satellite cells until a picture comparable with that seen in control tissue sections was visible. The functional significance of these changes in acid phosphatase activity within an altered metabolic environment induced by vagotomy is discussed.

Acid Phosphatase↗
PubMed2001

Changes in oxidative stress parameters and acid phosphatase activity in the pre-regressing and regressing tail of Indian jumping frog Polypedates maculatus (Anura, Rhacophoridae).

Activities of acid phosphatase (normal and Co2+-sensitive), superoxide dismutase and catalase and levels of lipid peroxidation, hydrogen peroxide were compared in the tails of tadpoles of stage III, XVIII, XXI and XXIII, respectively, of the Indian Jumping frog Polypedates maculatus. It is noticed that acid phosphatase activity (normal and Co2+-sensitive), and levels of lipid peroxidation and hydrogen peroxide increased during tail regression. There is also an increase in the level of superoxide dismutase and catalase in the regressing tail. A positive correlation between activity of acid phosphatase and lipid peroxidation, hydrogen peroxide and lipid peroxidation, acid phosphatase and hydrogen peroxide was noticed in the tail of tadpoles during different developmental stages, suggesting a critical interaction between reactive oxygen species and lysosomal activity during metamorphosis.

Acid Phosphatase↗
PubMed1976

An optimized continuous-monitoring procedure for semiautomated determination of serum acid phosphatase activity.

A continuous-monitoring method for measuring acid phosphatase activity with alpha-naphthyl phosphate as the substrate was critically evaluated and modified. Using partially purified prostatic acid phosphatase, we show that certain conditions for the assay must be satisfied to ensure linearity. These conditions include maintaining the pH between 5.6 and 5.9 and the addition of detergent to sustain linearity. The results obtained with alpha-naphthyl phosphate have been compared with those obtained by using p-nitrophenyl phosphate as substrate. When used with an automatic rate analyzer, the modified method is as sensitive but more reproducible.

Acid Phosphatase↗
PubMed1991

The effect of internal biliary drainage on bile pigment accumulation and acid phosphatase activity in human liver during obstructive jaundice.

The effect of internal drainage after biliary obstruction due to primary cholangiocarcinoma has been studied in seven human liver biopsies with respect to bile pigment accumulation and acid phosphatase activity. Enzyme activity was demonstrated at the light-microscopic level in unfixed cryostat sections using an incubation medium containing naphthol AS-BI phosphate as substrate, and hexazotised pararosaniline as simultaneous coupling agent, and at the ultrastructural level in fixed tissue blocks and chopped tissue sections using sodium beta-glycerophosphate as substrate and lead or cerium ions as capture reagent. Large amounts of bilirubin were found in cryostat sections of non-drained cholestatic livers, especially in pericentral areas. At these sites a high acid phosphatase activity was found. At the ultrastructural level, acid phosphatase activity was found only in the lysosomal compartment--possibly due to the procedure necessary for tissue processing. After internal biliary drainage, the amount of bilirubin diminished, with a concomitant decrease in acid phosphatase activity. The co-localization of accumulations of bile compounds and acid phosphatase activity indicates that lysosomes play a role in the breakdown of bile compounds.

Acid Phosphatase↗
PubMed1975

An ultrastructural study of acid phosphatase localization in Phaseolus vulgaris xylem by the use of an azo-dye method.

The localization of acid phosphatase during xylem development has been examined in the bean, Phaseolus vulgaris. The azo dye, the final reaction product, is initially prominent in the dictyosomes, vesicles apparently participating in secondary wall formation, and in the middle lamella of the young vessel element. Final reaction particles are also present in mitochondria, chloroplasts, and certain vacuoles and are sparsely scattered in the cytoplasm. At a later stage of vessel differentiation, the azo dye is concentrated in the disintegrating cytoplasm and along the fibrils of the partially hydrolysed primary wall and middle lamella. In the mature vessel element, the azo dye is still present along the disintegrated primary wall at the side of the vessel and covers the secondary wall. In the parenchyma cell adjacent to the vessel element, acid phosphatase localization is found in the dictyosomes, endoplasmic reticulum, mitochondria, small vacuoles, and the middle lamella. The controls from all stages of vessel element development were free of azo dye particles. The concentration of acid phosphatase along the secondary walls of the mature vessels and in the middle lamella between other cells indicates that this enzyme has other functions besides autolysis of the cytoplasm and primary cell wall. Acid phosphatase may participate in the formation of the secondary wall and may also have a role in the secretion and transport of sugars.

Acid Phosphatase↗
PubMed1977

[Electron-cytochemical study of acid phosphatase in the brain after death].

The activity of acid phosphatase in the rat and human brain was determined by the electron-cytochemical method. Lysosomes and lipofuchsin granules proved to possess enzymatic activity. Use of postmortem material showed the localization of acid phosphatase to remain unchanged at the remote periods after death.

Acid Phosphatase↗
PubMed1975

Histoenzymological mapping of acid phosphatase and 5-nucleotidase in the diencephalic and mesencephalic centers of Uromastix hardwickii.

The study deals with the histoenzymological mapping of acid phosphatase and 5-nucleotidase in the various nuclei of diencephalon and mesencephalon of Uromastix hardwickii. Almost all the nuclei and the fiber tracts reveal positive activity, both for acid phosphatase and 5-nucleotidase, althouh the intensity of the enzymatic activity presents great variations. Acid phosphatase preparations have generally revealed moderate or mild activity. On the contrary, the 5-nucleotidase preparations demonstrate the activity of a higher order. For this enzyme beside the nuclei, the commissures and fore-brain bundles are seen equipped with very intense activity. On the other hand, the commissures and fore-brain pundles present moderate activity for acid phosphatase. An attempt has been made to discuss the significance of the distribution of the enzymes at various locales.

Acid Phosphatase↗