[Alkaline phosphatase in neutrophil granulocytes and acid phosphatase in peripheral blood lymphocytes in premature infants].
Explore the source record for details and available documents.
Acid Phosphatase↗
SEARCH · Search PubMed
Results for “ACID PHOSPHATASE”
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.
Studies on leukocyte phosphatases. 3. Inhibition of leukocyte acid phosphatase by zinc.
Explore the source record for details and available documents.
Acid Phosphatase↗
[Possible existence of alternative secretion routes of acid phosphatase in the yeast Saccharomyces cerevisiae].
The secretion of different acid phosphatase forms into the growth medium was studied in the yeast Saccharomyces cerevisiae. The secretion of constitutive acid phosphatase highly correlated with the process of bud formation. This exoenzyme might be involved in the construction of the bud cell wall. Analysis of the rate, at which repressible acid phosphatase was excreted into the growth medium, as well as a negative correlation between its secretion and the process of bud formation were indicative of an additional route via which the repressible form of acid phosphatase was secreted. It is possible that yeast cells contain vesicles similar to "safe" vesicles in higher eukaryotic cells.
Acid Phosphatase↗
Rapid radioimmunoassay for prostate-specific acid phosphatase in human serum.
We describe a rapid radioimmunoassay for human prostatic acid phosphatase (EC 3.1.3.2) in serum, with use of monospecific antisera raised in rabbits against the primary highly purified acid phosphatase (pl 4.9) from human prostates, and with a second antibody-polyethylene glycol porecipitation. This radioimmunoassay is sensitive and can be performed within 5 h. Concentrations of the immunoreactive acid phosphatase in sera of healthy men (n = 394) ranged from 0.3 to 3.6 microgram/L (mean 1.94, SD 0.66 microgram/L). Concentrations of the enzyme in sera of men with benign prostatic hyperplasia (n = 56) or with carcinoma of nonprostatic origin (n = 24) were identical with those of the reference group. Serum concentrations of immunoreactive prostatic acid phosphatase of patients with occult, non-metastatic, and metastatic prostatic carcinoma varied from 1.7 to 9.3 (n = 9), 4.2 to 59.4 (n = 12), and 20 to 198 (n = 10) microgram/L, respectively. The amount of immunoassayable prostatic acid phosphatase was unchanged for at least five days in serum stored at 4 degrees C.
Acid Phosphatase↗
Alkaline and acid phosphatases in bone cells serve as phosphohydrolases at physiological pH in vivo: a histochemical implication.
Net activity of tissue-nonspecific alkaline phosphatase (TNAP) and acid phosphatase (ACP) remains to be determined since enzyme histochemistry has adopted biochemically determined optimal pH, which is not likely to represent local pH in vivo. The present study aimed to evaluate TNAP and ACP activities associated with bone cells at physiological pH. At the physiological pH of tissue fluid, intense phosphatase reactions were demonstrable in osteoblasts and osteoclasts as well as the bone matrix associated with osteoclasts. In fresh-frozen and freeze-substituted specimens, intense phosphatase reactions appeared at both alkaline and neutral pH along the entire surface of osteoblasts including the osteoidal surface, where TNAP was shown to be absent by immunohistochemistry. Combined specificity tests suggested that TNAP and ACP in bone cells can serve as phosphohydrolases at pH 7.3 and that reactions along the osteoidal surface of osteoblasts differ from that of TNAP and represent novel enzyme.
Acid Phosphatase↗
Preoperative serum acid phosphatase and alkaline phosphatase are not predictors of pathological stage and prostate-specific antigen failure after radical prostatectomy.
OBJECTIVE: To examine the utility and prognostic significance of enzymatic serum acid phosphatase (total acid phosphatase, TAP, and prostatic fraction of acid phosphatase, PFAP) and alkaline phosphatase (ALP) for staging, grading and outcome of patients who underwent radical retropubic prostatectomy (RRP) after the introduction of prostate-specific antigen (PSA) testing. PATIENTS AND METHODS: In all, 180 consecutive patients with clinically localized prostate cancer who underwent RRP with standard obturator lymph-node dissection between 1 January 1990 and 31 December 1995 were evaluated. Levels of TAP of > 5.4 IU/L, PFAP of > 1.2 IU/L and ALP of > 120 IU/L were classified as abnormally high. The relationship between abnormally high values and prostate cancer stage, grade and time to recurrence after RRP were calculated. The median follow-up was 86 months (approximately 7 years). RESULTS: Of the 180 patients, information about preoperative TAP, PFAP and ALP were available in 164, 163 and 154, respectively; TAP was abnormal in seven (4%), PFAP in 33 (20%) and ALP in only 13 (8%). None of the markers examined was associated with any variables of disease severity, as measured by pathological stage, Gleason score, perineural invasion, capsular penetration, positive margins, seminal vesicle involvement, and lymph node involvement. Abnormal TAP, PFAP or ALP were not associated with recurrence (P = 0.96, 0.45 and 0.41, respectively). In contrast, a PSA level of > 4 ng/mL was predictive of recurrence after RRP (P < 0.001). In the sample overall, 25 (14%) of the patients had recurrence and only one died from prostate cancer. CONCLUSIONS: Preoperative enzymatic serum TAP, PFAP and ALP levels are not predictors of the severity of disease or PSA disease-free recurrence after RRP.
Acid Phosphatase↗
Analysis of the acid phosphatases of rat sensory ganglia by isoelectric focussing on polyacrylamide gels.
The acid phosphatases of rat spinal and trigeminal ganglia have been separated by isoelectric focussing on polyacrylamide gels into two main classes with pI's of 7.1 and 5.4. A low-pI acid phosphatase is also present in the mouse but not in the guinea pig. Evidence is presented that in the rat the pI 5.4 enzyme represents the nonlysosomal acid phosphatase that has been identified histochemically in one population of sensory neurones. This pI 5.4 acid phosphatase is partly membrane-bound and is selectively depleted by capsaicin administration. In lumbar dorsal root ganglia the enzyme is selectively depleted by sectioning the sciatic nerve and undergoes rapid axonal transport, a greater amount being transported peripherally than centrally. The results are discussed with reference to the possible function of this nonlysosomal acid phosphatase.
Acid Phosphatase↗
[Purification of prostatic acid phosphatase from human seminal plasma].
Prostatic acid phosphatase has been isolated from human seminal plasma. The purification method utilizes gel filtration on Sephadex G100, ammonium sulfate precipitation and a series of chromatographical steps including concanavalin A Sepharose 4B, anion exchange and gel filtration chromatography. The final product appears homogenous when analyzed by gel filtration on Sephadex G100. It gives one major band on SDS polyacrylamide gels. The specific activity is similar to that obtained by other purification schemes. The yield of the method described above has allowed to set up a sensitive radioimmunoassay of prostatic acid phosphatase.
Acid Phosphatase↗
[Urological neoplasms and enzyme. IV. Studies on the alteration of lactic dehydrogenase, alkaline phosphatase, leucine aminopeptidase, and total acid phosphatase activities and LDH isozymes in experimentally induced renal tumors with dimethylnitrosamine].
Explore the source record for details and available documents.
Acid Phosphatase↗
Detection and localization of alkaline and acid phosphatases in the digestive system of the adult Catla catla (Hamilton), an Indian freshwater major carp by histochemical methods.
The localization and distribution of alkaline phosphatase (ALPase) and acid phosphatase (ACPase) in the various regions of the alimentary canal viz., buccopharynx, oesophagus, intestine, rectum and hepatopancreas of adult Catla catla have been studied by employing various histochemical techniques. ALPase activity was recorded in the various regions of the alimentary canal in the present study although its intensity of localization and distribution varies greatly. The highest ALPase activity was detected in the columnar epithelial cells of the intestine including their brush border, sub-mucosal layer as well as in the basement membrane while intense activity of the same was observed in the epithelial cells (stratified and columnar) of the buccopharynx and oesophagus, hepatic and pancreatic acinar cells. The intense localization of ALPase was also found in the nuclei of the epithelial cells (stratified and columnar), sub-mucosal connective tissue nuclei, hepatic cell nuclei, and sub-mucosal polysaccharide granules of the intestine. The moderate ALPase activity was detected in the neuroepithelial cells of the taste buds in the buccopharynx, cytoplasm of the epithelial cells (stratified and columnar) and muscularis layers. The blood vessels of the intestine and rectum also furnished moderate ALPase activity. The weak ALPase activity was noticed in the brush border of the rectum and also in the basement membrane. Intense ACPase activity was recorded in the striated border of the intestinal villi, while moderate activity of the same was detected in the nuclei of the stratified and columnar epithelial cells of the various regions of the alimentary canal as well as in the hepatic and pancreatic acinar cells. Very weak ACPase activity was localized in the cytoplasm of the stratified epithelial cells of the buccopharynx and oesophagus.
Acid Phosphatase↗
Characterization of intermediate-molecular-weight acid phosphatase from bovine kidney cortex.
The distribution of acid phosphatases of intermediate molecular weight was determined in various mammalian tissues. The intermediate-molecular-weight acid phosphatases (designated P-II-1 and 2) comprised about 25% of the p-nitrophenyl phosphatase activity in the supernatant of bovine kidney cortex homogenate. The P-II-1 and 2 purified 2,000 fold showed the pI values of 5.9 and 5.7, respectively, on isoelectric focusing. Apparent molecular weights of both P-II-1 and 2 were estimated to be 42,000 by Sephadex G-100 gel filtration and 44,000 by SDS-polyacrylamide disc gel electrophoresis. Both the enzymes catalyzed the hydrolysis of a wide variety of natural phosphomonoesters, except for the phosphoproteins phosphoserine and o-phosphocholine. The enzymes showed a high activity on pyridoxal phosphate, beta-glycerophosphate, and 2'-AMP. The optimum activity pH was near 5 with p-nitrophenyl phosphate, but was shifted to the neutral range when pyridoxal phosphate was the substrate. The cations Hg2+ and Ag+ had a marked inhibitory effect. Neither enzyme was inhibited significantly by L-(+)-tartrate or pCMB. The two other types of acid phosphatases, the high-molecular-weight (designated P-I) and low-molecular-weight (designated P-III), were also purified to homogeneity from bovine kidney cortex, and were compared with P-II from several aspects including substrate specificity and susceptibility to various compounds.
Acid Phosphatase↗
Comparison of enzyme assay and radioimmunoassay for the measurement of human acid phosphatase in cases of sexual assault.
We investigated whether a radioimmunoassay for prostatic acid phosphatase might be used as a more specific test for the identification of semen in samples from cases of sexual assault than the measurement of total acid phosphatase enzyme activity. The results of the measurement of acid phosphatase by enzyme assay in semen and vaginal swab extracts were compared with the results of the radioimmunoassay. It was found that the radioimmunoassay is a sensitive and more specific method than the enzymic determination of acid phosphatase. Incidentally we have found that a low concentration of an immunological cross reacting acid phosphatase is present in semen free vaginal swab extracts.
Acid Phosphatase↗
Purification and characterization of acid phosphatase from yellow lupin (Lupinus luteus) seeds.
Acid phosphatase (EC 3.1.3.2) from yellow lupin (Lupinus luteus) seeds was purified to homogeneity by ammonium sulphate fractionation, affinity chromatography, cation-exchange chromatography, gel filtration or reverse-phase HPLC. The enzyme is a dimer with the 50 kD and 44 kD subunits and contains 7.3% of carbohydrate, forming at least four oligosaccharide chains. The optimum pH for the enzyme is 5.4. The apparent Km for p-nitrophenyl phosphate was estimated to be 0.28 mM and Vmax = 1780 IU/mg of protein. The purified phosphatase has the highest specific activities reported for any plant acid phosphatases measured for any native or synthetic substrate. The enzyme has broad specificity; however, cyclic nucleotides, pyrophosphate or phytate are not cleaved. It is inhibited by molybdate, fluoride and phosphate. There is no change in the enzyme activity in the presence of EDTA, phenanthroline and tartrate.
Acid Phosphatase↗
Red cell acid phosphatase: another polymorphism correlated with Malaria?
The frequency of PC allele for acid phosphatase in fourteen Sardinian villages correlates positively with the altitude and negatively with past malarial morbidity and GdMed prevalence. The susceptibility towards hemolytic favism in Sardinian males with G6PD deficiency is dependent on the erythrocyte acid phosphatase and thalassemia phenotypes. Thalassemia trait exerts a protective action only in subjects carrying PA allele for acid phosphatase. The data suggest that the gradient for malaria morbidity directly or indirectly, through interactions with thalassemia and G6PD polymorphisms, mediated by the habit of eating Vecia faba, may have had a significant role in determining the heterogeneous distribution of acid phosphatase polymorphism in Sardinia. Besides malaria, other environmental factors related with altitude seem to have been very important in shaping the present pattern of distribution of both acid phosphatase and G6PD polymorphisms in Sardinia.
Acid Phosphatase↗
The demonstration of acid phosphatase in cultured 3T3 mouse cells.
Acid phosphatase has been demonstrated ultrastructurally in 3T3 and SV40-3T3 mouse cells using sodium beta-glycerophosphate and p-nitrophenyl phosphate as substrate. The former substrate only demonstrates the enzyme in lysosomes and elements of the Golgi apparatus while the latter demonstrates it in the cisternae of the endoplasmic reticulum and in the cell surface as well as at lysosomal sites. The significance of surface acid phosphatase activity is discussed in terms of sublethal autolysis.
4-Nitrophenylphosphatase↗
Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase.
We have partially purified an 18-kDa cytoplasmic protein from 3T3-L1 cells, which dephosphorylates pNPP and the phosphorylated adipocyte lipid binding protein (ALBP), and have identified it by virtue of kinetic and immunological criteria as an acid phosphatase (EC 3.1.3.2). The cytoplasmic acid phosphatase was inactivated by phenylarsine oxide (PAO) (Kinact = 10 microM), and the inactivation could be reversed by the dithiol, 2,3-dimercaptopropanol (Kreact = 23 microM), but not the monothiol, 2-mercaptoethanol. Cloning of the human adipocyte acid phosphatase revealed that two isoforms exist, termed HAAP alpha and HAAP beta (human adipocyte acid phosphatase), which are distinguished by a 34-amino acid isoform-specific domain. Sequence analysis shows HAAP alpha and HAAP beta share 74% and 90% identity with the bovine liver acid phosphatase, respectively, and 99% identity with both isoenzymes of the human red cell acid phosphatase but no sequence similarity to the protein tyrosine phosphatases (EC 3.1.3.48). HAAP beta has been cloned into Escherichia coli, expressed, and purified as a glutathione S-transferase fusion protein. Recombinant HAAP beta was shown to dephosphorylate pNPP and phosphoALBP and to be inactivated by PAO and inhibited by vanadate (Ki = 17 microM). These results describe the adipocyte acid phosphatase as a cytoplasmic enzyme containing conformationally vicinal cysteine residues with properties that suggest it may dephosphorylate tyrosyl phosphorylated cellular proteins.
3T3 Cells↗
An Arabidopsis mutant missing one acid phosphatase isoform.
Plant response to phosphorus starvation includes the increased production and secretion of acid phosphatase. We have isolated a mutant of Arabidopsis thaliana (L.) Heynh., phosphatase-underproducer 1 (pup1), that has reduced histochemical staining for acid phosphatase activity in roots of plants grown under phosphorus-starvation conditions. Although pup1 is defective in the production of one inducible acid phosphatase isoform, the most abundant inducible isoform is present. The pup1 mutants are able to respond to phosphorus-deficient conditions by an increase in overall levels of acid phosphatase activity, accumulation of anthocyanins, an increase of the root-to-shoot ratio, and changes in the partitioning of phosphorus between roots and shoots. The gross morphology of the mutants appears normal, except that a small difference in the root to shoot ratio was observed in plants grown under nonstressed conditions. The pup1 gene is incompletely dominant and it is located between 40.2 (+/- 6.2) and 44.9 (+/- 9.9) cM on chromosome 2. This mutant will be useful for determining the role of this acid phosphatase isoform in plant response to phosphorus starvation.
Acid Phosphatase↗
Toxoplasma gondii: characterization of a monoclonal antibody recognizing antigens of 36 and 38 kDa with acid phosphatase activity located in dense granules and rhoptries.
Acid phosphatase activity in Toxoplasma gondii was studied by electron microscopy and found in the rhoptries and dense granules. On Western blots, six bands were found to have acid phosphatase activity; a double band of 36-38 kDa showed the strongest activity. In order to raise monoclonal antibodies to antigens of potential importance in parasite invasion of the host cell, mice were immunized with live T. gondii of the cyst-forming ME119 isolate and later boosted with tachyzoites of the RH strain. One of the monoclonal antibodies, S16, recognized the 36- to 38-kDa antigen. Immunogold labeling and electron microscopy showed that the antigens were located in dense granules and rhoptries. Using immunoprecipitation with S16, SDS-PAGE, IEF, and Western blotting, we show that the 36- to 38-kDa rhoptry antigen recognized by S16 has acid phosphatase activity.
Acid Phosphatase↗