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At least 1,603 records · Page 89Linked to original sources
PubMed1988

Demonstration of acid phosphatase in Eimeria spp.: partial characterization of the enzyme in E. vermiformis.

Sporozoite extracts of E. vermiformis, E. stiedai, and E. tenella are rich in acid phosphatase activity. They contain specific enzyme activities equal to or greater than those reported for other highly virulent protozoan parasites. The absolute amount of enzyme activity per oocyst dramatically increases during sporulation of E. stiedai and E. vermiformis. Partial characterization of the acid phosphatase activity of E. vermiformis indicates that sporozoites account for greater than 92% of the total activity in sporulated oocysts, that the enzyme is resistant to inhibition by tartrate, and that it can be separated into two forms by anion exchange chromatography.

Acid Phosphatase↗
PubMed1984

Epithelial markers in prostatic, bladder, and colorectal cancer: an immunoperoxidase study of epithelial membrane antigen, carcinoembryonic antigen, and prostatic acid phosphatase.

Twenty prostatic adenocarcinomas, 20 transitional cell carcinomas of the bladder, and 20 colorectal adenocarcinomas were stained for epithelial membrane antigen, carcinoembryonic antigen, and prostatic acid phosphatase. Polyclonal affinity purified first and second antibodies and an indirect immunoperoxidase technique were used. All of the colorectal and bladder tumours and 16/20 prostatic tumours were positive for epithelial membrane antigen. All 20 colorectal, 7/20 bladder, and 5/20 prostatic tumours stained for carcinoembryonic antigen. All of the prostatic adenocarcinomas and none of the colorectal or bladder tumours were positive for prostatic acid phosphatase. These markers may be used to discriminate between tumours arising from these sites.

Acid Phosphatase↗
PubMed1964

ELECTRON MICROSCOPIC LOCALIZATION OF ACID PHOSPHATASE AND THIAMINE PYROPHOSPHATASE ACTIVITY IN HYPOTHALAMIC NEUROSECRETORY CELLS OF THE RAT.

Supraoptic nuclei in the hypothalamus of rats were fixed for the electron microscope by vascular perfusion with solutions of glutaraldehyde followed by post fixation with osmium tetroxide. Cytochemical methods for detection of acid phosphatase and thiamine pyrophosphatase activity have been applied to glutaraldehyde-fixed frozen sections containing the neurosecretory cells. The enzyme activities have been localized to certain Golgi cisternae. Acid phosphatase activity is present in the large (0.4 micro to 1.0 micro) granules or dense bodies which are surrounded by a single limiting membrane; both features characterize these structures as lysosomes. Smaller (0.1 micro) granules also present in the perikarya are generally unreactive towards enzyme activity and resemble in form the neurosecretory granules in the neurohypophysis.

Acid Phosphatase↗
PubMed1978

Phagocytic activity in the ischemic retinal pigment epithelial cells. An electronmicroscopic histochemical study of acid phosphatase.

The role of lysosomal enzymes in ischemic retinal pigment epithelial cells (RPE) of albino rabbits was examined with the modified Gomori technique for acid phosphatase. Ischemia was produced by cutting the lateral posterior ciliary artery and short posterior ciliary arteries (PCA). Five days after PCA-cut RPE in the ischemic region were disorganized by increased enzymatic digestion. In RPE of the border between the ischemic and normal region a lot of fragmented outer segments were phagocytosed 24 h to 7 days after PCA-cut. At this time phagosomes appeared much more frequently than in the normal retina, showing several variations in their shape, localization, and histochemical reaction. However, after 10 and 14 days, RPE in the border had a tendency to reduce the phagocytic activity. A strong acid phosphatase activity was encountered in the phagosomes of macrophages, which was considered to be derived from RPE, and seemed to play the major role in scavenging destructed retinal elements.

Acid Phosphatase↗
PubMed2004

The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold.

AphA is a periplasmic acid phosphatase of Escherichia coli belonging to class B bacterial phosphatases, which is part of the DDDD superfamily of phosphohydrolases. The crystal structure of AphA has been determined at 2.2A and its resolution extended to 1.7A on an AuCl(3) derivative. This represents the first crystal structure of a class B bacterial phosphatase. Despite the lack of sequence homology, the AphA structure reveals a haloacid dehalogenase-like fold. This finding suggests that this fold could be conserved among members of the DDDD superfamily of phosphohydrolases. The active enzyme is a homotetramer built by using an extended N-terminal arm intertwining the four monomers. The active site of the native enzyme, as prepared, hosts a magnesium ion, which can be replaced by other metal ions. The structure explains the non-specific behaviour of AphA towards substrates, while a structure-based alignment with other phosphatases provides clues about the catalytic mechanism.

Acid Phosphatase↗
PubMed1990

The histochemical localization of ATPase, cholinesterase and acid phosphatase activity in Culex pipiens (Diptera, Culicidae) larvae using a methacrylate embedding technique.

A method is described for the demonstration of ATPase, Cholinesterase and acid phosphatase activity in thin sections of mosquito larvae fixed in 1:9 v/v mixture of acetone and 10% neutral buffered formalin and embedded in hydroxyethyl methacrylate (HEMA). ATPase activity, observed as a black brown precipitate, was found in the brush border of gastric caeca and microvilli of columnar epithelial cells of the hind gut and Malpighian tubules. Some basal cell membrane activity could also be seen. Cholinesterase activity was found in thoracic and abdominal ganglia. The reaction product had a fine particulate appearance and predominated in the axonal processes. Azo dye reaction product indicative of acid phosphatase activity was found in the epithelial cells of the midgut and gastric caeca. Lysosomal and extra-lysosomal activity was observed, the larger secondary lysosomal sources predominating in the perinuclear region. The fixation regime and embedding procedure outlined has enabled a sub-cellular localization of enzymatic activities which is superior to that obtainable with conventional procedures.

Acid Phosphatase↗
PubMed1994

Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.

The three-dimensional structures of complexes of recombinant rat prostatic acid phosphatase with the transition-state analogs vanadate and molybdate were determined to 0.3-nm resolution using protein crystallographic methods. The overall structure of the enzyme remains unchanged upon binding of the metal oxyanions; only local conformational differences in the positions of some side chains at the active site were found. The metal oxyanions bind in an identical fashion at the active site with trigonal bipyramidal coordination geometry. The metal ion is within coordination distance of the His12 side chain which is located at one of the axial positions. The three equatorial oxygen atoms interact with the conserved residues Arg11, Arg15, Arg79 and His257. Within hydrogen-bonding distance of the axial oxygen atom is the side chain of the conserved residue Asp258. The implications of these results for the catalytic mechanism of acid phosphatase are discussed.

Acid Phosphatase↗
PubMed1991

Prostate irradiation does not affect the serum prostatic acid phosphatase level.

Twenty-nine consecutive patients with localized prostatic carcinoma were studied prospectively to assess the effect of radical pelvic irradiation on the serum prostatic acid phosphatase level (SPAPL). The doses of radiation given ranged from 64.00 to 66.00 Gy. SPAPLs were taken before, during and shortly after their treatment. No significant individual variations in SPAPLs were found. When patients with prostatic carcinoma show rises in serum prostatic acid phosphatase during or after pelvic irradiation, these are unlikely to be due to their treatment and occult pelvic nodal or bony disease should be considered.

Acid Phosphatase↗
PubMed1984

A combined assay of three lysosomal marker enzymes: acid phosphatase, beta-D-glucuronidase, and beta-N-acetyl-D-hexosaminidase.

A simplified and rapid method for simultaneous activity measurements of three lysosomal marker enzymes, acid phosphatase, beta-glucuronidase, and beta-N-acetyl-D-hexosaminidase is described. The incubation is carried out in a single test tube and stopped by adding an alkaline sodium dodecyl sulfate solution, thus avoiding centrifugations and allowing for higher Triton X-100 concentrations in the incubation media. Two products of the beta-glycosidases (phenolphthalein and 2-nitrophenolate) are measured spectrophotometrically at the respective wavelengths (555 and 420 nm), and one of the acid phosphatase products is quantitatively determined by measuring inorganic phosphate.

Acid Phosphatase↗
PubMed1990

Histochemical demonstration of non-specific esterases and non-specific acid phosphatases using menadiol substrates.

Although many synthetic substrates and methods are available for the histochemical detection of non-specific esterases and non-specific acid phosphatase, there are still further possibilities to investigate these hydrolases histochemically. This was shown for menadiol diacetate and menadiol diphosphate using tetrazolium salt, simultaneous azo-dye as well as metal salt methods in many rat tissues. In comparison, the azo-dye procedure with various Fast salts or hexazonium Pararosaniline or New Fuchsin delivered less satisfactory results; precisely localized stain in sufficient amounts was obtained for non-specific esterases using nitro BT, tetranitro BT or benzothiazolystyrylphthalhydrazidyl tetrazolium (BSPT) and for non-specific acid phosphatase with BSPT in the tetrazolium salt method or using cerium ions for phosphate trapping in the diaminobenzidine-nickel-hydrogen peroxide procedure.

Acid Phosphatase↗
PubMed1998

Cloning and characterization of the gene encoding a repressible acid phosphatase (PHO1) from the methylotrophic yeast Hansenula polymorpha.

A cloned cDNA, generated from mRNA isolates of phosphate-derepressed H. polymorpha cells, was identified to harbour an incomplete sequence of the coding region for a repressible acid phosphatase. The cDNA fragment served as a probe to screen a plasmid library of H. polymorpha genomic DNA. A particular clone, p606, of a 1.9-kb insert contained a complete copy of the PHO1 gene. Sequencing revealed the presence of a 1329-nucleotide open reading frame encoding a protein of 442 amino acids with a calculated M(r) of 49400. The encoded protein has an N-terminal 17-amino-acid secretory leader sequence and seven potential N-glycosylation sites. The leader cleavage site was confirmed by N-terminal sequencing of the purified enzyme. The nucleotide sequence is 48.9% homologous, the derived amino acid sequence 36% homologous to its Saccharomyces cerevisiae counterpart. The derived amino acid sequence harbours a consensus sequence RHGXRXP, previously identified as a sequence involved in active-site formation of acid phosphatases. The PHO1 promoter and the secretion leader sequence present promising new tools for heterologous gene expression.

Acid Phosphatase↗
PubMed1989

Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen.

Tartrate-resistant acid phosphatases types 5a and 5b were purified from human hairy cell leukemia spleen by sequential chromatography on Phenyl-Sepharose, CM-Sepharose, concanavalin A-Sepharose, FPLC Superose-12 and FPLC Mono-S. The purification over the original tissue extract was 1150- and 3300-fold, with a yield of 2.1% and 2.5%, respectively. Gel filtration indicated an Mr of about 30000 for both forms. There was a N-terminal sequence identity between the two enzymes. However, they appeared to be different as assessed by cation exchange chromatography and amino acid composition.

Acid Phosphatase↗
PubMedDate not supplied

Human seminal biochemistry: fructose, ascorbic acid, citric acid, acid phosphatase and their relationship with sperm count.

Seminal concentration of fructose, ascorbic acid, citric acid and acid phosphatase were measured in azoospermic, oligozoospermic and control males. No significant differences were found among the groups evaluated. The data obtained in the present study suggest that in the absence of infection and androgen deficiency, the failure of the germinal line of the testis is not correlated with alterations of the adnexal glands.

Acid Phosphatase↗
PubMed1992

Prostate adenocarcinoma using Gleason scores correlates with prostate-specific antigen and prostate acid phosphatase measurements.

To evaluate a relationship between Gleason scores of histopathology of prostate carcinoma and concurrent serum prostate-specific antigen (PSA) and prostate acid phosphatase (PAP) values, 65 men with prostate carcinoma were studied. These patients' cumulative Gleason scores were obtained by totaling the primary and secondary patterns, resulting in two groups: 42 patients received high (6-10) and 23 received low (2-5) Gleason scores. Serum PSA and PAP values were measured by radioimmunometric assay 1 to 7 days before surgical procedures or biopsy for prostate carcinoma. Mean serum PSA for patients in the high Gleason score group was 134.39 ng/mL (normal range: 0 to 4), and the mean serum PSA for patients in the low Gleason score group was 23.62 ng/mL. Mean serum PAP for patients with high scores was 28.08 ng/mL (normal range: 0 to 5), and the mean serum PAP for patients with low scores was 18.19 ng/mL. Patients with high Gleason scores showed significantly greater elevation of serum PSA than those with low Gleason scores (P = .047), using two samples to test for groups having unequal variants. Prostate acid phosphatase levels of patients with high scores were not significantly higher than the levels in patients with low scores (P = .60). These results indicate that PSA levels but not PAP levels correlate with Gleason scores.

Acid Phosphatase↗
PubMed1984

Acid phosphatase: its influence on the management of carcinoma of the prostate.

Of 343 patients who underwent pelvic lymph node dissection during treatment for carcinoma of the prostate 25 had persistently elevated serum enzymatic acid phosphatase levels preoperatively: 15 (60 per cent) had metastases to the pelvic lymph nodes and 10 (40 per cent) had negative nodes. Bone metastases occurred in 10 of 12 (83 per cent) and 5 of 7 patients (71 per cent), respectively, who were followed for a minimum of 2 years. Of the 318 patients with normal serum enzymatic phosphatase levels 70 (22 per cent) had positive nodes. A persistently elevated serum enzymatic acid phosphatase level in patients with proved carcinoma of the prostate, with elimination of infrequent causes of enzyme elevation, indicates metastases and has significant implications regarding staging and, thus, therapy of this disease.

Acid Phosphatase↗
PubMed1976

A new heat-stable acid phosphatase test for mycobacteria.

The heat-stable (70degrees C) acid phosphatase test performed by the method of Kind and King is a simple method for differentiating Mycobacterium kansasii, M. marinum, M. gastri, M. nonchromogenicum, and M. triviale from other slowly growing mycobacteria, and M. fortuitum from other rapidly growing acid-fast bacilli.

Acid Phosphatase↗
PubMed1991

Hydrochlorothiazide inhibits parathormone-stimulated increase in plasma tartrate-resistant acid phosphatase in mice.

The inhibitory effect of hydrochlorothiazide (HTZ) on parathormone-induced bone changes in mice was studied with the aid of the analysis of plasma calcium and tartrate-resistant acid phosphatase. We have found that HTZ alone had no effect on plasma tartrate-resistant acid phosphatase (Tr-ACP), phosphate, and creatinine concentration. Parathormone (PTH) administration increased plasma Tr-ACP from 15.00 +/- 1.50 to 20.62 +/- 2.35 U/liter in intact mice. The increase of plasma Tr-ACP in HTZ-treated mice after PTH administration was not significant. The plasma calcium was affected in a way similar to Tr-ACP. HTZ reduced the sensitivity of bone to resorbing effects of PTH, using Tr-ACP as a useful biomarker of bone resorption.

Acid Phosphatase↗