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PubMed1978

Purification of human prostatic acid phosphatase by affinity chromatography and isoelectric focusing. Part I.

The main isoenzyme of human prostatic acid phosphatases was purified by affinity chromatography on L(+)-tartrate linked to agarose and by isoelectric focusing. The enzyme was a single protein when examined by polyacrylamide gel electrophoreses, either as a native protein or in the presence of sodium dodecyl sulfate. The analytical recovery of enzyme activity was 19%. The specific activity was 40 18 mumol/(min X mg) for hydrolysis of 5.5 mmol/liter p-nitrophenyl phosphate at pH 4.8 and 37 degrees C. The purification factor was as great as 1900. The molecular weight of the enzyme as measured by gel filtration was 109 000 and by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate 54 000, indicating that the enzyme had been isolated in the dimer form. By this method we have achieved the best purification of human prostatic acid phosphatase so far.

Acid Phosphatase↗
PubMed1984

Radioimmunoassay for prostatic acid phosphatase in early prostatic carcinoma.

A radioimmunoassay procedure has been used to measure prostatic acid phosphatase in the serum of 46 patients with intracapsular carcinoma of the prostate. The results obtained did not differ significantly from those obtained in a control group of similar size. It is concluded that the radioimmunoassay procedure for measurement of prostatic acid phosphatase has no advantage over enzyme activity measurements for the detection of early prostatic carcinoma.

Acid Phosphatase↗
PubMed1992

Interaction of porcine uterine fluid purple acid phosphatase with vanadate and vanadyl cation.

Uteroferrin, the purple acid phosphatase from porcine uterine fluid, is noncompetitively inhibited by vanadate in a time-dependent manner under both aerobic and anaerobic conditions. This time-dependent inhibition is observed only with the diiron enzyme and is absent when the FeZn enzyme is used. The observations are attributed to the sequential formation of two uteroferrin-vanadium complexes. The first complex forms rapidly and reversibly, while the second complex forms slowly and results in the production of catalytically inactive oxidized uteroferrin and V(IV), which is observed by EPR. The redox reaction can be reversed by treatment of the oxidized enzyme first with (V(IV)) and then EDTA to generate a catalytically active uteroferrin. Multiple inhibition kinetics suggests that vanadate is mutually exclusive with molybdate, tungstate, and vanadyl cation. The binding site for each of these anions is distinct from the site to which the competitive inhibitors phosphate and arsenate bind. The time-dependent inhibition by vanadate of uteroferrin containing the diiron core represents a new type of mechanism by which vanadium can interact with proteins and gives additional insight into the binding of anions to uteroferrin.

Acid Phosphatase↗
PubMed1985

Histochemistry of the juxtaglomerular apparatus in the toad Bufo bufo. Acid phosphatase activity of the epitheloid cells in the glomerular afferent arterioles.

Histochemical techniques for acid phosphatase activity applied to kidney tissue of the toad Bufo bufo demonstrate that a high enzyme activity is present in the dense granules of the proximal tubule cells, but also in the media cells in the wall of the glomerular afferent arterioles. The acid phosphatase activity is confined to the characteristic granules in these juxtaglomerular cells, which therefore are lysosomal in nature.

Acid Phosphatase↗
PubMed1978

Comparative study on the activity, pH optimum and thermal stability of some glycosidases and acid phosphatase from pig and mule leukocytes.

1. alpha-D-mannosidase, beta-D-galactosidase, alpha-L-fucosidase, beta-N-acetylgalactosaminidase, alpha-D-glucosidase and acid phosphatase activities were studied in circulating blood leukocytes from Sus scropha var. domestica L. (pig) and Equus asinus x caballus (mule) by spectrophotometric procedures using p-nitrophenyl derivatives as substrates and three different buffer solutions. 2. The highest specific activity corresponds to acid phosphatase. The specific activities of the glycosidases, all relatively close together in all cases, were low in comparison with that of phosphatase. 3. Generally, each of the above-mentioned enzymes shows one common peak for the pH optimum between 3.5 and 6.0, except alpha-D-glucosidase, which shows two peaks. 4. The pH optima values are generally similar in three buffer solutions employed. 5. Specific activities of the studied enzymes show a parallelism in leukocytes from both pig and mule. Also, this parallelism is observed in their pH optima values. 6. Thermal stability of alpha-D-mannosidase is high whereas that of acid phosphatase is low, in both materials. For other enzymes, differences in the thermal stability was observed according to their source.

Acid Phosphatase↗
PubMed2000

Phosphorylation of nucleosides by the mutated acid phosphatase from Morganella morganii.

A novel nucleoside phosphorylation process using the food additive pyrophosphate as the phosphate source was investigated. The Morganella morganii gene encoding a selective nucleoside pyrophosphate phosphotransferase was cloned. It was identical to the M. morganii PhoC acid phosphatase gene. Sequential in vitro random mutagenesis was performed on the gene by error-prone PCR to construct a mutant library. The mutant library was introduced into Escherichia coli, and the transformants were screened for the production of 5'-IMP. One mutated acid phosphatase with an increased phosphotransferase reaction yield was obtained. With E. coli overproducing the mutated acid phosphatase, 101 g of 5'-IMP per liter (192 mM) was synthesized from inosine in an 88% molar yield. This improvement was achieved with two mutations, Gly to Asp at position 92 and Ile to Thr at position 171. A decreased K(m) value for inosine was responsible for the increased productivity.

Acid Phosphatase↗
PubMed1979

[Acid phosphatase in the nerve tissue exposed to local vibration].

The results of examinations for acid phosphatase in the spinal neurons of cats treated by vibration are presented. The animals were subjected to various periods of vibration with parameters of 20 Hz frequency and 2 mm amplitude. The activity of acid phosphatase in the nervous tissue was found to depend upon the duration of vibration: after a short-term treatment the activity of the enzyme was reduced insignificantly, after a long-term treatment a sharp reduction of the enzyme activity was observed in most cells.

Acid Phosphatase↗
PubMed1977

Isozymes of acid phosphatase in normal and cancerous human prostatic tissue.

The supernatants of the homogenates from normal and cancerous human prostatic tissue run on polyacrylamide gel electrophoresis have 2 major electrophoretic bands when stained for prostatic acid phosphatase. The ratios of the electrophoretically distinguishable isoenzymes differ in normal and cancerous tissues. Similar distinctions between isoenzymes in normal and cancerous prostates are observed following column chromatographic separation or isoelectric focusing. The faster electrophoretic band can be separated by diethylaminoethyl cellulose column chromatography or by isoelectric focusing into at least five fractions with different electrophoretic mobilities. We could not find any differences in normal and cancerous tissues among these subfractions of the faster-moving electrophoretic band. Analysis by gel electrophoresis does not show association between these fractions after chromatographic or isoelectric separation of the prostatic acid phosphatase fractions. Quantitative, but no qualitative, differences in prostatic acid phosphatase isozymes occur in normal versus cancerous prostates.

Acid Phosphatase↗
PubMedDate not supplied

Histochemical and ultrastructural alterations of lysosomes and acid phosphatase reaction in human chronic hypoxic myocardium.

Histochemical and ultrastructural alterations of lysosomes and acid phosphatase reaction were assayed in myocardial human specimens from patients with some acquired and congenital cardiac affections and cardiac failure class II-IV (after NYHA classification). The optic and electron microscopic study of the acid phosphatase (the main lysosomal marker) activity reveals that the intensity and the distribution of the reaction were correlated with the degree of heart failure, being maximum at the IVth degree. The electron microscopic analysis of the lysosomal vacuolar apparatus emphasizes various changes also correlated with the intensity of hypoxia.

Acid Phosphatase↗
PubMed1976

[Serum acid phosphatase levels following prostatic massage (author's transl)].

We find an elevation of serum acid phosphatase levels 5 min after prostatic massage in only 10% of patients with prostatic adenoma. This increase is caused by stored prostatic secretion being pressed into the blood vessels. 60 min later these serum levels decrease. With some other patients a slower increase of phosphatase levels occurs; this increase, however, lasts for hours. This kind of increase is caused by prostatic fluid being forced into the interstitium where it is slowly absorbed. A combination of both kinds leads to a curve with two peaks; this could be demonstrated in two cases. No difference was seen in reaction of total acid phosphatase and prostatic phosphatase levels. The increase of phosphatase levels following prostatic massage was no sign of prostatic carcinoma.

Acid Phosphatase↗
PubMed2001

Acid phosphatase activity in different organs as a marker of acute pancreatitis.

The aim of the experiment was to establish and quantify the changes in the activity of acid phosphatase in the pancreas, liver, spleen and kidneys during the course of experimental pancreatitis. The experiment was carried out on 65 male rats of Wistar strain, whose weight varied from 250 to 350 g. The animals were standard fed. They drank only water 24 hours before operation. The rats were randomly divided into three groups: A--intact animals group which were not operated and were used to mark initial biochemical parameters (15 rats), B--the experimental group of animals which were injected by retrograde way with sodium taurocholate into the common bile-pancreatic duct to induce acute necrotic pancreatitis (50 rats). After laparotomy an injection needle was inserted into the common bile-pancreatic duct via the proximal part of the duodenum (Aho's method). After 2, 6, 12, 24, 48 hours rats were anaesthetised again, and thoracotomy was performed by taking blood for amylase determination from the left ventricle of the heart. Then the animals were given an overdose of ketamine, and the organs were removed during laparotomy and frozen at the temp. of -20 degrees C. Alpha-amylase activity in the blood serum was determined by the enzymatic method. Acid phosphatase activity was assayed by spectrophotometric methods using a substrate which releases 4-methyloumbeliferol reacting with the enzyme. The authors concluded that the activity of membranous fraction of acid phosphatase changed non-specifically over the course of experimentally induced acute pancreatitis in rats, but statistically significant difference was found in the enzyme's activity during different periods of pancreatitis only in the pancreas and in the liver.

Acid Phosphatase↗
PubMed1987

Analytical and physiological characteristics of prostate-specific antigen and prostatic acid phosphatase in serum compared.

We did a comparative analysis of the physiological and analytical properties of prostate-specific antigen (PSA), acid phosphatase (ACP; EC 3.1.32) activity, and acid phosphatase antigen (PAP) in serum. The PSA assay is sensitive to 0.2 microgram/L and demonstrates good linearity (y = 1.01x + 0.74). The CV was 3.9% at 40 micrograms/L, 8.0% at 3.1 micrograms/L. PSA and PAP are less stable at 4 degrees C than at -20 degrees C. Serum PAP and ACP concentrations showed large intra-individual fluctuations (average CVs of 22% and 24%, respectively), which were not observed with PSA measurements (average CV 6.2%). We saw significant correlation with the magnitude of physiological change when analytes were compared for serially collected split samples [y(PSA) = 0.14x(PAP) + 0.00, r = 0.767], which indicates that a common factor is influencing this variation. The excellent analytical performance, tissue specificity, and small degree of intra-individual variance are characteristics that favor the measurement of PSA in serum for monitoring patients with prostatic cancer.

Acid Phosphatase↗
PubMed1990

Alkaline and acid phosphatase activity in murine femoral bone marrow following X-irradiation, or X-irradiation and repopulation with syngenic or allogeneic bone marrow or marrow stroma cells.

The activity of alkaline and acid phosphatases in the bone marrow from the femoral cavity was investigated in the following groups of mice: (1) normal (non-irradiated); (2) irradiated with 600 R; (3) irradiated and repopulated with syngeneic bone marrow; (4) irradiated and repopulated with syngeneic marrow stroma; (5) non-irradiated, infused with allogeneic bone marrow (host versus graft reaction, HvG); (6) irradiated and repopulated with allogeneic bone marrow (graft versus host reaction, GvH). In addition, the activity of alkaline and acid phosphatases was examined in bone marrow stromal cultures. In irradiated animals the activity of both enzymes was lower than in non-irradiated ones, repopulation with syngeneic bone marrow restoring it to normal. Repopulation with allogeneic marrow (GvH) resulted in a very deep reduction of alkaline, but not acid, phosphatase. It is postulated that the decrease in bone marrow alkaline phosphatase activity can be a sensitive test for the early GvH reaction, preceding such parameters as splenomegaly. Marrow stroma cultured in vitro also showed very low alkaline phosphatase activity.

Acid Phosphatase↗
PubMed1998

Improved method for measuring tartrate-resistant acid phosphatase activity in serum.

We describe an improved method for the kinetic measurement of tartrate-resistant acid phosphatase (TrACP; EC 3.1.3.2) activity in serum. Of the TrACP derived from erythrocytes, platelets, and macrophages (osteoclasts and others), that from the first two sources is also resistant to fluoride, whereas skeletal TrACP is sensitive to fluoride. Thus, osteoclast-derived TrACP can be measured specifically by exploiting its sensitivity to fluoride. We measured the activity of tartrate-resistant and fluoride-sensitive acid phosphatase (TrFsACP) by using 2,6-dichloro-4-acetylphenyl phosphate as substrate at pH 6.2. The activity of TrFsACP in serum was increased by adding hexadimethrine bromide (Polybrene) to the reaction mixture. This method was not influenced by hemolysis with hemoglobin concentrations as great as 0.9 g/L. The mean +/- SD values of TrFsACP activity by this method were 20.4 +/- 2.8 and 16.4 +/- 2.3 U/L for young (ages 20-29 years) men (n = 34) and women (n = 50), respectively. The highest mean TrFsACP activity was found among children younger than 15 years, followed by that in elderly subjects (older than 60).

Acid Phosphatase↗
PubMed2004

The class C acid phosphatase of Helicobacter pylori is a 5' nucleotidase.

The results from purification and characterization studies of the hppA gene product of Helicobacter pylori confirm its identification as a class C acid phosphatase. The hppA gene of H. pylori ATCC strain 49503 was amplified and modified by PCR, cloned into pET21b, and overexpressed in Escherichia coli. The recombinant protein was liberated from membranes and purified (16x) to apparent homogeneity with cation exchange and Ni-chelate chromatography resulting in a recovery of 39% of total starting activity. The recombinant acid phosphatase exhibited a denatured molecular mass of 24 kDa by SDS-PAGE. Phosphatase activity in both crude and purified samples could be renatured and detected after SDS-PAGE. The native molecular mass of recombinant enzyme was approximately 72 kDa by gel filtration chromatography on Superdex 75. While phosphate and tartrate had little effect on phosphatase activity, molybdate, vanadate, and EDTA had significant inhibitory effects on enzymatic activity. Phosphomonoesterase activity for hydrolysis of p-nitrophenylphosphate (pNPP) as well as other substrates was enhanced in the presence of divalent cations including Cu(2+), Ni(2+), Co(2+), and Mg(2+). Recombinant HppA had narrow substrate specificity with highest activity for arylphosphates and significant activity for 5' nucleoside monophosphates. The pH optimum for enzyme activity was 4.6 and 5.2 for purine and pyrimidine 5' monophosphates, respectively. The affinity constants for the 5' nucleoside monophosphates were found to be 0.5-1 mM. Results from this study confirm HppA inclusion in the class C acid phosphatases and led to its identification as a 5' nucleotidase.

5'-Nucleotidase↗
PubMed1987

Identification of rat osteoclasts in bone smears with quantification of acid phosphatase activity in vitamin D deficiency.

Vitamin D deficiency may depress bone formation but its effect on bone resorption is not well defined. As an index of bone resorption, the activity of acid phosphatase, a lysosomal enzyme found in osteoclasts, was quantitated in situ from a bone tissue smear preparation. Activity of the enzyme, measured by integrative microdensitometry increased linearly from 25 to 60 min. The distribution of activity in osteoclasts quantitated appeared to follow a normal distribution with a median value of 0.19 integrated optical density units. Animals treated with vitamin D or 1,25 dihydroxycholecalciferol had significantly increased activity of acid phosphatase in osteoclasts compared to animals which were vitamin D deficient. The increase of acid phosphatase activity averaged 63%. Vitamin D or its metabolites may have a permissive effect on the action of parathyroid hormone or act directly to increase bone resorption.

Acid Phosphatase↗
PubMed1985

Biochemical studies on a novel vanadate- and molybdate-sensitive acid phosphatase from human epidermis.

A novel vanadate- and molybdate-sensitive human skin epidermal acid phosphatase was purified and characterized. The enzyme was extracted from epidermal sheets with a 0.1% Triton X-100 solution buffered at pH 7.0. The purification procedure consisted of molecular permeation chromatography on Sephadex G-200 followed by chromatography on hydroxylapatite using an ammonium sulfate gradient. The molecular weight of the enzyme was 82,000 and the isoelectric point was at pH 5.6. At the optimum pH (5.1) the enzyme hydrolyzed most rapidly 1-naphthyl phosphate (Km = 0.28 mM) and 4-nitrophenyl phosphate (Km = 0.28 mM). In general, the best substrates had an aromatic leaving group. Fluoride (Ki = 39 microM; noncompetitive) and phosphate (competitive) inhibited by binding to different binding sites of the enzyme. The most potent inhibitors were vanadate (Ki = 1.9 X 10(-6)M), tungstate (Ki = 1.4 X 10(-7)M), and molybdate (Ki = 2.0 X 10(-9)M). Chemical modification and kinetic experiments suggested that the activity of the enzyme is based on imidazole, tyrosyl, and carboxyl groups. Benzoyl peroxide was a relatively potent inhibitor (Ki = 5.0 X 10(-5)M; noncompetitive). This enzyme resembled the prostatic acid phosphatase with regard to substrate specificity, inhibition characteristics, and functional groups.

Acid Phosphatase↗
PubMed1980

Biochemical and electrophoretic properties of acid phosphatase isozymes and their distribution in cell functions from neoplastic prostatic tissues.

The various acid phosphatase isozymes can be distinguished on the basis of their biochemical properties or their net electrical charge. Four main groups of isozymes hydrolyze beta-glycerophosphate: the fastest-moving form seemed to be related to the cancerous state. The quantity of enzyme, either in the whole homogenate or in cytoplasmic fractions was not a useful criteria for cancer, however, while the distribution of acid phosphatase in subcellular structures was characteristic in cancer cases. Cell fractions were obtained by differential centrifugation, but were contaminated with prostatic secretions.

Acid Phosphatase↗