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PubMed1972

Purification and characterization of acid phosphatase V from Aspergillus nidulans.

Acid phosphatase V of Aspergillus nidulans was purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. The enzyme demonstrated a charge microheterogeneity on starch and acrylamide gel electrophoresis, but proved to be homogeneous on ultracentrifugation and gel filtration. Phosphatase V was found to be a classic acid orthophosphoric monoester phosphohydrolase, and it cleaved p-nitrophenylphosphate, glucose-6-phosphate, and uridine-5'-monophosphate at maximal rates. It was inhibited by fluoride, borate, and molybdate ions, and demonstrated end-product inhibition by inorganic phosphate. Metallic ions or cofactors were not required for activity. The molecular weight was estimated to be 100,000, the S(20,w) was calculated to be 4.1, and the pH optimum was found to be 6.1.

Acid Phosphatase↗
PubMed1979

[Cytochemical and biochemical determination of acid phosphatase activity in yeasts].

Optimal conditions of the cytochemical assay for acid phosphatase in protoplasts and whole cells of S. cerevisiae have been described. Dimethyl sulfoxide was used to increase the permeability of the yeast cell envelope. In the yeast cells, grown up to the end of the exponential phase, acid phosphatase is shown to be located mainly in the central vacuole and on the cell envelope surface. A considerable activity of acid phosphatase is demonstrable on the surface of the plasma membrane and within adjacent vesicles that represent, presumably, part of the endoplasmic reticulum. Acid phosphatase can be considered as a marker enzyme for yeast cell vacuoles.

Acid Phosphatase↗
PubMedDate not supplied

Design of spindle poisons activated specifically by prostatic acid phosphatase (PAP) and new methods for PAP cytochemistry.

By taking advantage of the structural requirements of the substrates for prostatic acid phosphatase (PAP), which consist of steric hindrance and the presence of basic nitrogen in the molecule, potential cytotoxic agents (spindle poisons) are being designed that will become enzyme activated specifically by PAP. Colchicine has been converted to colchiceinamides of substituted ethanolamines and o-phosphoethanolamines. The rate of hydrolysis of the latter by human prostatic tissue as compared to the rate of hydrolysis by human kidneys (P/K ratio) is given and indicates a significant degree of specificity for PAP. Some preliminary toxicity data in mice are also given. New thiocolchicine derivatives with phosphates on ring B are also being prepared for study and some preliminary toxicity data are given. The observation in biochemical experiments that phosphorylcholine is a very specific substrate for PAP has led us to develop specific cytochemical methods for PAP for both light and electron microscopy. Preliminary observations are given and good evidence is provided that PAP is not a lysosomal enzyme, unlike other acid phosphatases. Furthermore, PAP is to other acid phosphatases what the cholinesterases are to other esterases. Since the acid phosphatase that is able to hydrolyze phosphorylcholine is characteristic of prostatic epithelium, this is the acid phosphatase that is referred to be the designation of PAP. Other acid phosphatases (both lysosomal and nonlysosomal) in prostatic epithelial cells are not demonstrated by this substrate and hence are not included in this designation.

Acid Phosphatase↗
PubMed1986

Biosynthesis of two developmentally distinct acid phosphatase isozymes in Dictyostelium discoideum.

The presence of a common antigenic determinant on the Dictyostelium discoideum acid phosphatase isozyme 1 (ap 1), and the absence of this determinant on the isozyme ap2 enables separation of the two isozymes. This separation is accomplished by removal of ap1 from samples with a common antigen monoclonal antibody followed by immunoprecipitation of ap2 with an acid phosphatase monoclonal antibody. Application of this separation scheme on cells pulse-labeled early (2 h) and late (18 h) in the developmental cycle reveal that ap1 protein synthesis occurs only early in development and that the protein remains stable throughout development, whereas ap2 protein synthesis occurs only late in development. Furthermore, pulse-chase experiments during both early and late development reveal that both isozymes of acid phosphatase are initially synthesized as precursor molecules (Mr = 60,000) which are then processed to mature forms (Mr = 58,000). The processing event(s) for acid phosphatase begin in less than 5 min compared to 25-30 min for Dictyostelium alpha-mannosidase and 10-15 min for Dictyostelium beta-glucosidase. Endoglycosidase H and Endoglycosidase F treatment of both isozymes reveals identical cleavage patterns for ap1 and ap2, indicating that the amount of carbohydrate on both molecules is equivalent. Preliminary studies to identify modification differences reveal that fucose is not present on either isozyme; however, sulfate is present on the ap1 isozyme and absent on the ap2 isozyme. These results suggest that differences in the modification of newly synthesized acid phosphatase at different times during the Dictyostelium life cycle result in the appearance of two distinct acid phosphatase isozymes.

Acid Phosphatase↗
PubMed1995

Immunoassay of a tartrate-resistant acid phosphatase in serum.

A tartrate-resistant acid phosphatase (TRACP) was purified from cord plasma by use of cation-exchange chromatography (carboxymethyl Sepharose), gel-filtration chromatography (Sephacryl S-200), and preparative isoelectric focusing. After raising polyclonal antibodies to the purified TRACP in rabbit, we used the antiserum to develop an ELISA. The antiserum cross-reacted with an extract of bone, but not with extracts of spleen, erythrocytes, platelets, or osteoblasts or with prostatic acid phosphatase. With this ELISA we determined the concentration of serum TRACP in healthy men to be 197 (61-301) micrograms/L (median and range). Serum TRACP concentrations were significantly higher in children and postmenopausal women and in patients with chronic renal failure, hyperparathyroidism, or hyperthyroidism. Estrogen replacement therapy of postmenopausal women for 3-6.5 months decreased their serum TRACP concentration by 70%.

Acid Phosphatase↗
PubMed1994

Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Modulation of osteoclast adhesion in vitro.

The tartrate-resistant acid phosphatase (TRAP) of skeletal osteoclasts was found to partially dephosphorylate the bone matrix phosphoproteins osteopontin (OPN) and bone sialoprotein (BSP). TRAP also partially dephosphorylated metabolically [32P]PO4-labeled OPN as well as BSP, whereas comparable amounts of either alkaline phosphatase or prostatic acid phosphatase, at their respective pH optima, were ineffective, indicating a certain preference of TRAP for these phosphoprotein substrates. It has previously (Flores, M., Norgärd, M., Heinegård, D., Reinholt, F. P., and Andersson, G. (1992) Exp. Cell Res. 201, 526-530) been shown that osteoclasts bind to OPN as well as to BSP coated onto glass. We can now show that the partially dephosphorylated proteins no longer support osteoclast binding. These results indicate that the secretion of TRAP from osteoclasts into the resorption area could exert a regulatory influence on the attachment of the cells to the bone surface. This could imply roles in the development of ruffled borders and/or in the regulation of osteoclast motility on the bone surface.

Acid Phosphatase↗
PubMed1986

Acid phosphatase deficient mutants of Schizosaccharomyces pombe are defective in tyrosine uptake.

The uptake of tyrosine and arginine into wild type and acid phosphatase deficient mutants (pho 1) of Schizosaccharomyces pombe was investigated. All 11 pho 1-alleles tested exhibited a reduced tyrosine uptake and impaired uptake cosegregated with the lack of acid phosphatase activity. Kinetic analyses using wild type cells grown in high phosphate medium (acid phosphatase repressed) and low phosphate medium (acid phosphatase derepressed) showed staturation kinetics for tyrosine with a KM of about 2 x 10(-4) M for both media and a V of about 5 nmol min-1 mg-1 and 2 nmol min-1 mg-1 for derepressed and repressed cells respectively. The pho 1-118 strain completely lacked this saturable uptake system for tyrosine. Preliminary evidence suggests that tyrosine uptake may be via a general amino acid permease system and we conclude that mutations in the structural gene of acid phosphatase which abolish enzyme activity lead to a loss of this uptake system. In contrast to tyrosine, arginine uptake seems not to be significantly affected either by different acid phosphatase levels in wild type cells or by the pho 1-118 mutation.

Acid Phosphatase↗
PubMed1995

Acid phosphatase activity and phosphorus nutrition in Scots pine needles.

From March to October, acid phosphatase activity and phosphorus (P) concentration were measured in four needle age classes of the upper and lower crowns of fertilized and unfertilized Scots pine (Pinus sylvestris L.) trees. Negative correlations between acid phosphatase activity and P concentration were observed in current-year needles and in needles in the upper part of the crown, whereas there was a positive correlation between enzyme activity and P concentration in older needles and in needles in the lower part of the crown. In May and October, needles of all ages showed increased acid phosphatase activity. The most sensitive response of acid phosphatase activity to phosphate supply and phosphorus status of the whole tree was seen in current-year needles on the first whorl where a 300% increase in acid phosphatase activity was observed in response to a decrease in foliar P concentration of 1.7-1.8 mg P g(DW) (-1).

Journal Article↗
PubMed2003

A novel antimicrobial protein isolated from potato (Solanum tuberosum) shares homology with an acid phosphatase.

The nucleotide and amino acids sequences for AP(1) will appear in the GenBank(R) and NCBI databases under accession number AY297449. A novel antimicrobial protein (AP(1)) was purified from leaves of the potato ( Solanum tuberosum, variety MS-42.3) with a procedure involving ammonium sulphate fractionation, molecular sieve chromatography with Sephacryl S-200 and hydrophobic chromatography with Butyl-Sepharose using a FPLC system. The inhibition spectrum investigation showed that AP(1) had good inhibition activity against five different strains of Ralstonia solanacearum from potato or other crops, and two fungal pathogens, Rhizoctonia solani and Alternaria solani from potato. The full-length cDNA encoding AP(1) has been successfully cloned by screening a cDNA expression library of potato with an anti-AP(1) antibody and RACE (rapid amplification of cDNA ends) PCR. Determination of the nucleotide sequences revealed the presence of an open reading frame encoding 343 amino acids. At the C-terminus of AP(1) there is an ATP-binding domain, and the N-terminus exhibits 58% identity with an/the acid phosphatase from Mesorhizobium loti. SDS/PAGE and Western blotting analysis suggested that the AP(1) gene can be successfully expressed in Escherichia coli and recognized by an antibody against AP(1). Also the expressed protein showed an inhibition activity the same as original AP(1) protein isolated from potato. We suggest that AP(1) most likely belongs to a new group of proteins with antimicrobial characteristics in vitro and functions in relation to phosphorylation and energy metabolism of plants.

Acid Phosphatase↗
PubMed2004

The insect hemolymph protein HP19 mediates the nongenomic effect of ecdysteroids on acid phosphatase activity.

The activity of acid phosphatase (ACP) in insect fat bodies is stimulated by the steroid hormone 20-hydoxyecdysone (20E) in vivo. However, in fat bodies kept in culture, a factor from the hemolymph is required to enhance the ACP activity. We identified the factor as a protein with a molecular mass of 19 kDa (HP19) from the hemolymph of a lepidopteran insect, the rice moth, Corcyra cephalonica. Western analysis of hemolymph proteins with denaturing and non-denaturing PAGE using antibodies raised against HP19 suggest that this protein exists as a monomer. It is synthesized by the hind gut-associated lobular fat body of the larvae and is released into the hemolymph. The stimulatory effect of HP19 on the ACP activity is developmentally regulated and exhibits its maximal effect shortly before the onset of metamorphosis. We cloned the HP19 cDNA by immunoscreening a hind gut-associated lobular fat body cDNA expression library. Analysis of the amino acid sequence shows that HP19 belongs to the family of glutathione S-transferase (GST) like proteins. However, affinity-purified GST from Corcyra failed to show any mediation effect on 20E-stimulated ACP activity, and HP19 lacks GST enzymatic activity. Notably, HP19 mediates the hormone-stimulated ACP activity in intact fat body tissue and homogenates even in the presence of inhibitors of transcription and translation, suggesting a nongenomic mode of action. In addition, we show that HP19 inhibits the 20E-induced phosphorylation of the hexamerin receptor protein.

Acid Phosphatase↗
PubMed1986

[Phosphotyrosine]protein phosphatase in rat brain. A major [phosphotyrosine]protein phosphatase is a 23 kDa protein distinct from acid phosphatase.

A [phosphotyrosine]protein phosphatase (PTPPase) was purified almost to homogeneity from rat brain, with [32P]p130gag-fps, an oncogene product of Fujinami sarcoma virus, as substrate. The characteristics of the purified preparation of PTPPase were as follows: the enzyme was a monomer with a molecular mass of 23 kDa; its optimum pH was 5.0-5.5; its activity was not dependent on bivalent cations; its activity was strongly inhibited by sodium vanadate, but was not inhibited by ZnCl2, L(+)-tartrate or NaF; it catalysed the dephosphorylation of [32P]p130gag-fps, [[32P]Tyr]casein, p-nitrophenyl phosphate and L-phosphotyrosine, but did not hydrolyse [[32P]Ser]tubulin, L-phosphoserine, DL-phosphothreonine, 5'-AMP, 2'-AMP or beta-glycerophosphate significantly. During the purification, most of the PTPPase activity was recovered in distinct fractions from those of conventional low-molecular-mass acid phosphatase (APase), which was reported to be a major PTPPase [Chernoff & Li (1985) Arch. Biochem. Biophys. 240, 135-145], from DE-52 DEAE-cellulose column chromatography, and those two enzymes could be completely separated by Sephadex G-75 column chromatography. APase also showed PTPPase activity with [32P]p130gag-fps, but the specific activity was lower than that of PTPPase with molecular mass of 23 kDa, and it was not sensitive to sodium vanadate. These findings suggested that PTPPase (23 kDa) was the major and specific PTPPase in the cell.

Acid Phosphatase↗
PubMed1983

Quality control of acid phosphatase assay improved by direct reconstitution of lyophilized control materials with citric acid.

Current quality control of assays of acid phosphatase (EC 3.1.3.2) with thymolphthalein substrate is inadequate when certain control-suppliers' instructions are followed for reconstituting and stabilizing human lyophilized control material. If such materials are reconstituted with a citric acid solution, then stored frozen, control vial-to-vial variability is minimized, as are losses of activity in freshly reconstituted controls and losses during room-temperature storage of the control material. Effects of pH of the reconstituting solution on the acid phosphatase activity of human lyophilized controls are also discussed.

Acid Phosphatase↗
PubMed1999

Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean.

Purple acid phosphatases comprise a family of binuclear metal-containing acid hydrolases, representatives of which have been found in animals, plants, and fungi. The goal of this study was to characterize purple acid phosphatases from sweet potato tubers and soybean seeds and to establish their relationship with the only well-characterized plant purple acid phosphatase, the FeIII-ZnII-containing red kidney bean enzyme. Metal analysis indicated the presence in the purified sweet potato enzyme of 1.0 g-atom of iron, 0.6-0.7 g-atom of manganese, and small amounts of zinc and copper. The soybean enzyme contained 0.8-0.9 g-atom of iron, 0.7-0.8 g-atom of zinc per subunit, and small amounts of manganese, copper, and magnesium. Both enzymes exhibited visible absorption maxima at 550-560 nm, with molar absorption coefficients of 3200 and 3300 M(-1) cm(-1), respectively, very similar to the red kidney bean enzyme. Substrate specificities were markedly different from those of the red kidney bean enzyme. A cloning strategy was developed based on N-terminal sequences of the sweet potato and soybean enzymes and short sequences around the conserved metal ligands of the mammalian and red kidney bean enzymes. Three sequences were obtained, one from soybean and two from sweet potato. All three showed extensive sequence identity (>66%) with red kidney bean purple acid phosphatase, and all of the metal ligands were conserved. The combined results establish that these enzymes are binuclear metalloenzymes: Fe-Mn in the sweet potato enzyme and Fe-Zn in soybean. The sweet potato enzyme is the first well-defined example of an Fe-Mn binuclear center in a protein.

Acid Phosphatase↗
PubMed1983

Inhibition by dithionite and reactivation by iron of the tartrate-resistant acid phosphatase in bone of osteopetrotic (ia) rats.

The staining intensity and inhibitor sensitivity of acid phosphatase activity was determined histochemically in various tissues of normal and ia rat pups by the use of freeze-dried whole body sections. Activity was determined using alpha-naphthylphosphate as substrate and hexazonium pararosaniline as coupler. Sections from ia rats (6 and 24 days old) showed markedly higher enzyme activity in bone than sections from normal littermates. However, there were no differences between ia and normal pups in acid phosphatase activity in soft tissues and developing teeth. Preincubation of sections with 1-100 mM sodium dithionite (an iron-binding agent) caused a dose-related inhibition of enzyme activity in bone of ia and normal pups, but only slight inhibition of activity in soft tissues. Partial restoration of the dithionite-inhibited activity in bone was achieved by subsequent preincubation in 1 mM FeCl2. Addition of 100 mM sodium tartrate to the staining solution of non-preincubated sections caused almost complete inhibition of activity in soft tissues and the developing teeth but no inhibition of the activity in bone that was sensitive to sodium dithionite. These data indicate a) that sodium dithionite can be used as a specific histochemical inhibitor of the tartrate-resistant acid phosphatase and b) that the source of increased acid phosphatase activity in bone from ia rats is mostly from the tartrate-resistant acid phosphatase.

Acid Phosphatase↗
PubMed1977

Determination of serum acid phosphatase in Gaucher's disease using 4-methylumbelliferyl phosphate.

We describe a new assay that is useful for identifying individuals who may be affected with Gaucher's disease. The assay involves the determination of serum acid phosphatase activity using the fluorogenic substrate 4-methylumbelliferyl phosphate. The assay measures acid phosphatase activity at pH 6.0 in the presence of 3.0 M 2-mercaptoethanol and requires a 5 microliter serum sample and a 15-min incubation period. Under these conditions, 2-mercaptoethanol preferentially inhibited the acid phosphatase activity in control serum but did not inhibit the elevated acid phosphatase present in the serum of patients with Gaucher's disease. Using this assay, we observed a 5-50-fold elevation in serum acid phosphatase activity in 8 patients with the adult, non-neuropathic form of Gaucher's disease when compared to control serum assayed under the same conditions. Serum from several heterozygotes free from pathology exhibited normal acid phosphatase activity when assayed at pH 6.0 in the presence of 2-mercaptoethanol. Acid phosphatase activity in serum from patients with prostatic cancer can be distinguished from that in Gaucher serum on the basis of the well-documented sensitivity of the former to inhibition by sodium tartrate. A serum sample from a patient with Niemann-Pick disease exhibited a mild elevation in tartrate-resistant acid phosphatase activity so that conclusive diagnosis of Gaucher's disease requires assaying leukocytes or fibroblasts from suspected patients for glucocerebroside:beta-glucosidase activity.

Acid Phosphatase↗
PubMed1990

Change in the isoenzyme composition of acid phosphatase in murine peritoneal macrophages exposed to or infected with Trypanosoma cruzi.

The effect of infection with Trypanosoma cruzi on the activity and isoenzyme composition of acid phosphatase within individual murine peritoneal macrophages maintained in vitro was studied. Concentrations of acid phosphatase activity and number of intracellular parasites were quantitated by using a computer-assisted cytospectrophotometry system. Changes in the isoenzyme composition of macrophages during infection with T. cruzi were detected by comparing the patterns of acid phosphatase levels between macrophages treated in the absence and presence of an enzyme inhibitor. It was observed that the concentration levels of acid phosphatase activity in macrophages did not change significantly by infection with T. cruzi. Also, the concentration levels of acid phosphatase activity did not change in macrophages uninfected but exposed to T. cruzi. On the other hand, the isoenzyme composition of acid phosphatase did change in macrophages exposed to or infected with T. cruzi. These results demonstrate that Trypanosoma cruzi affects the acid phosphatase composition of macrophages.

Acid Phosphatase↗
PubMed1983

Differential diagnostic value of acid phosphatase and beta-glucuronidase in acute leukaemia.

Differential diagnostic importance of acid phosphatase and beta-glucuronidase reactions was studied in bone marrow smears of 52 patients with acute leukaemias. Both reactions showed either diffuse or simultaneously diffuse and granular positivity in the medullary blast cells of 34 patients suffering from ANLL. A strong diffuse positivity of acid phosphatase suggested the possibility of AMOL. Beta-glucuronidase and acid phosphatase reactions were exclusively granular in every positive case of ALL. Increased acid phosphatase activity was found in T-ALL while beta-glucuronidase showed increased activity also in (non-T, non-B)-ALL on several occasions.

Acid Phosphatase↗
PubMedDate not supplied

Substrate response in acid phosphatase activity of Pseudomonas pseudomallei and Pseudomonas cepacia, with special reference to tyrosine phosphatase.

The substrate response in acid phosphatase activity of Pseudomonas pseudomallei and Pseudomonas cepacia was examined with different phosphate esters including hexose phosphates and phosphoaminoacids in a whole cell assay system. The enzymatic activity against each substrate was evaluated in terms of percent activity to that against para-nitrophenyl phosphate set as 100. A remarkable finding was that the phosphatase reaction was the highest with phosphotyrosine or phosphoserine as substrate showing 180% activity. This tyrosine phosphatase activity was resistant to heating at 60 C for 20 min and inhibited greatly by 0.1% ZnCl2. Pseudomonas cepacia showed the same pattern of substrate response and the same characteristics of tyrosine phosphatase activity.

Acid Phosphatase↗