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PubMed1984

Protein, cholesterol, acid phosphatase and aspartate aminotransaminase in the seminal plasma of turkeys (Meleagris gallopavo) producing normal white or abnormal yellow semen.

Turkeys which produce yellow semen have abnormal ductuli efferentes' epithelial morphology, with blebbing of cytoplasmic material into the ductal lumen. This could possibly increase the activity or concentration of seminal plasma components. In the present study, seminal plasma from 270 Large White breeder turkeys was evaluated for protein and cholesterol concentrations and the activities of acid phosphatase and asparate aminotransaminase. In a separate experiment, protein concentrations of turkey seminal plasma were estimated by biuret or Bradford methods. Bradford estimates were 46.6% less than those obtained with the biuret assay, using bovine serum albumin as the standard. Estimates of seminal plasma protein concentration in the main study were obtained using the Bradford method, and should be adjusted accordingly when compared with other studies using the biuret technique. Abnormal yellow seminal plasma, compared to normal white seminal plasma, had elevated levels of total protein and cholesterol and increased activities of acid phosphatase and aspartate aminotransaminase. Overall means were: 14.3 mg/ml, 38.9 mg/dl, 232.6 IU/ml, 81.0 IU/ml, respectively. Correlation coefficients for cholesterol concentration, acid phosphatase and aminotransaminase activity with protein concentration were +0.65, 0.70 and 0.50 (P less than 0.0001), respectively. Specific activities of both enzymes showed a significant reduction as seminal plasma protein increased, indicating a disproportionate increase in proteins other than these enzymes in yellow seminal plasma.

Acid Phosphatase↗
PubMed1975

[The behavior of unspecific acid phosphatase in the human gingiva before and after the effect of aminofluorides].

The authors determined the activity of the unspecific acid phosphatase in dental papillae excised from healthy subjects and individuals afflicted with periodontitis before and after the action of Elmex fluid. Clinically and histologically, the authors observed a regression of the inflammation. The possible causes are discussed. The total activity of acid phosphatase in the interdental papilla showed no significant changes, but the various tissue layers behaved differently. No permanent lesion will result from the wetting of the papillary and marginal gingiva which occurs during topical application of Elmex fluid to the surfaces of teeth.

Acid Phosphatase↗
PubMed1977

Isozymic changes of acid phosphatase and esterase in regenerating rat liver after partial hepatectomy in relation to cell differentiation.

Activities and isozyme patterns of acid phosphatase and esterase were studied in rat liver at different intervals after partial hepatectomy to clarify the grade of immaturity of normal regenerating liver cells as a control for the unlimited proliferation of hepatoma cells. Acid phosphatase and esterase activities in the liver were elevated during a 12-hr period after hepatectomy, while their isozyme patterns did not change from those of immature liver. Similar findings were also observed in the liver of sham-operated rats. Eighteen hours after the operation, at the S phase before cell division, the isozyme pattern of these enzymes began to shift from an adult liver-type to an immature one resembling those of the infant liver 3 weeks after birth rather than those of newborn or fetal liver. Two or three days after partial hepatectomy, the isozymes characteristic of an immature liver type were more apparent. Although enzyme activities mostly returned to the normal adult level one week after the operation, the isozyme patterns did not completely return to those of an adult liver. These results indicate that despite the rapid proliferation of liver cells, the grade of cell differentiation of the regenerating liver after partial hepatectomy is much nearer to that of the normal adult liver rather than that of the fetal liver.

Acid Phosphatase↗
PubMed2004

Sweet potato acid phosphatase immobilized on glutaraldehyde-activated aminopropyl controlled-pore glass: activation, repeated use and enzyme fatigue.

Sweet potato acid phosphatase was covalently coupled with glutaraldehyde to aminopropyl controlled-pore glass, and used as a pre-column enzyme reactor. The immobilized enzyme reactor (IMER) was continuously operated using an automated chromatographic detection system we developed. Functional evaluation of the IMER was carried out by injecting ten samples on the same day at an injection amount of 1.25 nmol (62.5 nmol per ml) using riboflavin sodium phosphate (FMNs) as a substrate, and by prolonged use for ten months. The IMER exhibited decreased activity after repeated use for a total of 3000 samples, but about 75% of its original activity remained. The conversion rate of FMNs to riboflavin by IMER was increased from 89 to 97% by adding citrate, ethylenediaminetetraacetic acid disodium salt, etc., but especially by adding citrate. The increased conversion of FMNs to riboflavin due to the addition of citrate was probably not due to the chelation of heavy metal ions by citrate. We also investigated complex formation of acid phosphatase with the substrate FMNs using surface plasmon resonance to determine the effect of citrate on the processes of association and/or dissociation between the enzyme and substrate. Enzyme fatigue was also observed during the course of prolonged and repeated use.

Acid Phosphatase↗
PubMedDate not supplied

[Acid phosphatase activity during digestion in the anintestinal turbellaria Convoluta convoluta].

Studies have been made on changes in the activity of acid phosphatase during the digestion in the turbellaria C. convoluta. The increase of the enzymic activity of cytoplasm of the peripheral parenchyma at the initial stages after feeding (6 hours, 1 day) and gradual decrease of this activity at later stages (2,4 and 7 days) were noted. The presence of acid phosphatase in the nuclei and cytoplasm of cells of the central parenchyma at all stages of the digestive cycle is explained by degeneration of these cells which is associated with holocrine secretion of the digestive enzymes.

Acid Phosphatase↗
PubMed1982

A simple and rapid method for osteoclast identification using a histochemical method for acid phosphatase.

A detailed description of a simple technique for acid phosphatase demonstration in osteoclast cells is presented. The method is short, relatively uninvolved and allows the use of undecalcified bone sections. All materials and chemicals used are commercially available. The sections were stained histochemically using naphthol AS-B1 phosphoric acid as a substrate and counter stained with Mayer's Haematoxylin. Sections prepared by this method showed good results and enabled accurate measurement of osteoclast counts.

Acid Phosphatase↗
PubMed1982

The cellular organization of fibroblastic cells and macrophages at regions of uncalcified cartilage resorption in the embryonic chick femur as revealed by alkaline and acid phosphatase histochemistry.

Resorption of uncalcified cartilage in the embryonic chick femur appears to be mediated by two types of mononuclear cells. One cell type lies flattened and adherent along the surface of the cartilage matrix into which it extends cellular processes. Cytological characteristics of a large, euchromatic nucleus containing a nucleolus, and cytoplasm containing moderate to extensive amounts of rough endoplasmic reticulum indicate that these are protein synthetic cells. Macrophages, characterized by a pleomorphic shape and cytoplasm containing numerous mitochondria and vesicles, comprise the second cell type. These may be seen lying in contact with cartilage matrix, but are more likely located in the nonhematopoietic marrow adjacent to resorbing cartilage, where they establish close cellular associations with protein synthetic cells. Alkaline and acid phosphatase histochemical studies differentiate these two cellular types. Marrow alkaline phosphatase activity is restricted to the cartilage-marrow interface from which it diffuses a short distance into cartilage matrix, but does not diffuse into nearby marrow. Intracellular alkaline phosphatase is present only in protein synthetic cells that line the surface of cartilage, and thus appears to be produced by these cells. Acid phosphatase positive macrophages are scattered throughout the marrow, but are found in greatest concentrations in the region of cartilage resorption. They are rarely in direct contact with cartilage, and there is no evidence that acid phosphatase is released from these cells. The relative localizations and the presence of cellular interactions of these two cell types suggests that protein synthetic cells may be of fibroblastic origin, and may play a primary role in cartilage degradation, while macrophages, in keeping with biochemical evidence, play an adjunct or possibly a regulative role.

Acid Phosphatase↗
PubMed1977

Heterogeneity of acid phosphatase, beta-glucuronidase, and alpha-naphthyl-acetate esterase in normal and leukaemic lymphocytes.

Comparative study of isoenzymic patterns of acid phosphatase, beta-glucuronidase and alpha-naphthyl acetate esterase of normal and chronic lymphocytic leukaemia (CLL) lymphocytes was carried out by means of polyacrylamide gel electrophoresis. The isoenzymograms of acid phosphatase and beta-glucuronidase of leukaemic cells were similar to that of normal lymphocytes. However, different patterns were found in the case of alpha-naphthyl acetate esterase. Two prominent anodal bands were present in CLL lymphocytes; these bands were either absent or very weak in normal cells.

Acid Phosphatase↗
PubMed2000

Transgenic mice overexpressing tartrate-resistant acid phosphatase exhibit an increased rate of bone turnover.

Tartrate-resistant acid phosphatase (TRAP) is a secreted product of osteoclasts and a lysosomal hydrolase of some tissue macrophages. To determine whether TRAP expression is rate-limiting in bone resorption, we overexpressed TRAP in transgenic mice by introducing additional copies of the TRAP gene that contained the SV40 enhancer. In multiple independent mouse lines, the transgene gave a copy number-dependent increase in TRAP mRNA levels and TRAP activity in osteoclasts, macrophages, serum, and other sites of normal low-level expression (notably, liver parenchymal cells, kidney mesangial cells, and pancreatic secretory acinar cells). Transgenic mice had decreased trabecular bone consistent with mild osteoporosis. Measurements of the bone formation rate suggest that the animals compensate for the increased resorption by increasing bone synthesis, which partly ameliorates the phenotype. These mice provide evidence that inclusion of an irrelevant enhancer does not necessarily override a tissue-specific promoter.

Acid Phosphatase↗
PubMed1999

Prognostic role of serum prostatic acid phosphatase for 103Pd-based radiation for prostatic carcinoma.

PURPOSE: To establish the prognostic role of serum enzymatic prostatic acid phosphatase (PAP) in patients treated with palladium (103Pd) and supplemental external beam irradiation (EBRT) for clinically localized, high-risk prostate carcinoma. METHODS AND MATERIALS: One hundred twenty-four consecutive patients with Stage T2a-T3 prostatic carcinoma were treated from 1992 through 1995. Each patient had at least one of the following risk factors for extracapsular disease extension: Stage T2b or greater (100 patients), Gleason score 7-10 (40 patients), pretreatment prostate specific antigen (PSA) >15 ng/ml (32 patients), or elevated serum PAP (25 patients). Patients received 41 Gy conformal EBRT to a limited pelvic field, followed 4 weeks later by a 103Pd boost (prescription dose 80 Gy). Biochemical failure was defined as a PSA greater than 1 ng/ml (normal <4 ng/ml). RESULTS: The overall, actuarial freedom from biochemical failure at 4 years after treatment was 79%. In Cox-proportional hazard multivariate analysis, the strongest predictor of failure was elevated pretreatment acid phosphatase (p = 0.02), followed by Gleason score (p = 0.1), and PSA (p = 0.14). CONCLUSION: PAP was the strongest predictor of long-term biochemical failure. It may be a more accurate indicator of micrometastatic disease than PSA, and as such, we suggest that it be reconsidered for general use in radiation-treated patients.

Acid Phosphatase↗
PubMed1976

[Studies on the activity, properties and isoenzymes of acid phosphatase in the erythrocytes of swine, horse, dog, cat, duck and chicken].

Acid phosphatase of erythrocytes of several species was investigated, with three isozymes having been recorded from swine (three types), three (two types) from horse, four (one type) from dog, two (two types) from cat, two (three types) from duck, and two (one type) from fowl. The Michaelis constant of the enzyme varied between 3.5 and 5 X 10(-4) M for the species involved. The species, however, differed slightly for the optimum pH of the enzyme. The average enzymatic activities were (5.68 +/- 0.42 for dog, 4.46 +/- 1.0 for horse, 3.8 +/- 0.24 for swine, 3.72 for cat, 2.5 +/- 0.62 for duck, and 1.9 +/- 0.8 for fowl. All values are units per gram haemoglobin. Even relatively low concentrations (0.2 or 1 mM) of copper, mercury, and cadmium ions were found to be strong inhibitors of the acid erythrocyte phosphatase.

Acid Phosphatase↗
PubMed1989

The 18 kDa cytosolic acid phosphatase from bovine live has phosphotyrosine phosphatase activity on the autophosphorylated epidermal growth factor receptor.

In this paper we demonstrate that the cytosolic low-Mr acid phosphatase purified from bovine liver has phosphotyrosine protein phosphatase activity on 32P-autophosphorylated epidermal growth factor (EGF) receptor. This activity was significantly inhibited by orthovanadate and p-hydroxymercuribenzoate; the latter result indicates that free sulfhydryl groups are required for phosphotyrosine phosphatase activity. The enzyme was active in a broad pH range, with maximum activity between pH 5.5 and 7.5. The apparent Km for 32P-EGF receptor dephosphorylation was 4 nM. The enzyme appeared to be specific for phosphotyrosine in that it dephosphorylated the autophosphorylated EGF receptor and L-phosphotyrosine, but not 32P-Ser-casein, L-phosphoserine or L-phosphothreonine. These data suggest that the cytosolic low-Mr acid phosphatase might play a regulatory role in EGF receptor-dependent transmembrane signalling.

Acid Phosphatase↗
PubMed1999

Two-site immunoassays for osteoclastic tartrate-resistant acid phosphatase based on characterization of six monoclonal antibodies.

Tartrate-resistant acid phosphatase (TRAP), an enzyme expressed in bone-resorbing osteoclasts, is secreted into the circulation during bone resorption. We used six monoclonal antibodies (MAbs) to optimize direct two-site fluoroimmunoassays for determining serum TRAP concentrations. Four of the MABs, 1F1, 2H1, 4E6, and 5C1, were raised against recombinant human TRAP, and the other two, O1A and J1B, against human bone TRAP. 2H1, J1B, and O1A appeared to be highly specific for TRAP. 1F1 and 4E6 were poor in recognizing bone TRAP and were not useful in the assay. 5C1, while having a good affinity for the bone enzyme, was not specific. Serum TRAP is relatively stable, because 7 days of storage of serum samples at 4 degreesC and -20 degreesC or five thawing-freezing cycles, did not change the TRAP concentration detected using the two-site assays. All studied assays detected an increase in serum TRAP concentrations of postmenopausal women compared with premenopausal women, the difference being highest with MAB pairs 2H1-5C1 and O1A-J1B. These results suggest that serum TRAP may be a useful bone resorption marker, and the MAB pairs 2H1-5C1 and O1A-J1B may be useful in determining the bone resorption rate.

Acid Phosphatase↗
PubMed1978

Regulation of acid phosphatase synthesis in Saccharomyces cerevisiae.

In Saccharomyces cerevisiae-136ts (Hutchison, H.T., Hartwell, L.H. and McLaughlin, C.S. (1969) J. Bacteriol. 99, 807--814) derepressed acid phosphatase was almost exclusively located outside the permeability barrier. Only a minor part of the activity was associated with the protoplasts; about half of it (48%) in the soluble fraction, the rest bound to the internal (45%) and plasma (7%) membranes. The activity found in the membranes of derepressed cells decreased by 30--40% after addition of inorganic phosphate or cycloheximide suggesting that this activity is the precursor of the external enzyme. The alkaline phosphatase activity level could not be modified by changes in the concentration of inorganic phosphate. Acid phosphatase was not synthesized if the cells were transferred to a low phosphate medium at the moment of incubation at 37 degrees C or in the presence of cycloheximide at 23 degrees C. The data suggested that enzyme formation is the result of the transcription and translation of a specific gene(s) and not the activation of a proenzyme. Inorganic phosphate did not inhibit the translation of mRNA though it may act at the level of the transcription.

Acid Phosphatase↗
PubMed1997

Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas.

PURPOSE: Keratoconus is characterized by thinning and scarring of the central region of the cornea. The authors have shown, in corneas obtained from patients with keratoconus, that lysosomal enzyme activities are elevated, whereas levels of protease inhibitors such as alpha 1-proteinase inhibitor (alpha 1-PI) are reduced. This study was undertaken to examine further the gene expression of cathepsin G, acid phosphatase, and alpha 1-PI in keratoconus corneas. METHODS: Corneal buttons were collected from patients with keratoconus, normal subjects, and patients with other corneal diseases. In situ hybridization was performed on paraffin sections using a tritium-labeled probe for cathepsin G or alpha 1-PI. Competitive polymerase chain reaction (PCR) was used to determine the messenger RNA (mRNA) levels for lysosomal acid phosphatase and alpha 1-PI in epithelial and stromal cells of keratoconus corneas. RESULTS: Silver grains, indicative of positive in situ hybridization products, were observed in all three cell types of normal corneas for both DNA probes. Compared with normal and other diseased controls, the labeling was enhanced for cathepsin G but was diminished for alpha 1-PI in the epithelium of keratoconus corneas. Competitive PCR showed that the mRNA level for acid phosphatase was higher and that the mRNA level for alpha 1-PI was lower in keratoconus corneas. CONCLUSIONS: These results indicate that the mRNA level for degradative enzymes in increased and that for alpha 1-PI it is reduced in keratoconus corneas. This study provides the first evidence that the altered expression of multiple enzymes and inhibitors in keratoconus occurs at the gene level. Furthermore, it implicates a possible role of coordinated transcriptional regulation of gene expressions in keratoconus.

Acid Phosphatase↗
PubMed1985

Sequential changes of sensory neuron (fluoride-resistant) acid phosphatase in dorsal root ganglion neurons following neurectomy and rhizotomy.

Five to seven days after sciatic nerve section in rats, fluoride-resistant acid phosphatase (FRAP) expression in dorsal root ganglion (drg) neurons was markedly decreased. The decrease was in contrast to increased acid phosphatase which has been reported to occur in other neurons after nerve section. FRAP expression in ganglion neurons subsequently increased 14-21 days after nerve section; this preceded the restitution of enzyme expression in the spinal cord substantia gelatinosa. FRAP expression in drg neurons was not decreased after dorsal root section.

Acid Phosphatase↗
PubMed1990

The structural gene coding for thiamin-repressible acid phosphatase in Schizosaccharomyces pombe.

The pho4 gene of the fission yeast Schizosaccharomyces pombe is regulated by thiamin. The nucleotide sequence of this gene is given here and it is shown that it matches the amino acid sequence of thiamin-repressible acid phosphatase, corroborating genetic evidence that pho4 represents the structural gene of this enzyme. The gene codes for a protein of 463 amino acids in length and shows regions of strong similarity with the phosphate-repressible acid phosphatase of Schizosaccharomyces pombe. The enzyme has a cleavable signal sequence 18 amino acids long and carries nine potential N-glycosylation sites.

Acid Phosphatase↗
PubMed1980

[Coupling of 1-naphthol with fast-red-TR. Studies on the optimization of a continuous determination of acid phosphatase, I. (author's transl)].

In the course of studies on the optimization of a method for the continuous determination of acid phosphatase, the coupling of 1-naphthol with fast-red-TR was investigated: 1. In the presence of detergents or protein, the detection reaction gives a linear response for spectral absorption in the range 0-1 against concentration. 2. The reaction between naphthol and fast-red-TR salt is first order with respect to 1-naphthol. 3. The half life time for the coupling must be less than 0.5 min, in order to keep the lag phase of the reaction below 2 min. 4. Shortening of the coupling half life time (increase in the rate of the indicator reaction) was achieved by increasing the fast-red concentration and pH-value, and by alterations, within certain limits, of ionic strength and the concentration of protein and/or detergents. 5. Development of the chromophore depends on time and the presence of proteins and/or detergents. Reliable measurements are only possible at the isosbestic point of the chromophore. In the presence of albumin, these are 460 nm and 390 nm. 6. Reproducible formation of the chromophore requires the presence of protein (albumin); replacement by detergents is possible to a limited extent. 7. In order to avoid a time-dependent bathochromic effect, buffer materials should be present in the lowest possible concentration: citrate buffer 0.2 mol/l; acetate buffer 0l.4 mmol/l. 8. By coupling with fast-red-TR salts, serum proteins result in increased positive values (apparent enzyme activity) up to 2.6 U/l, depending on the measurement wavelength for the chromophore. 9. Molar absorption coefficients for wavelengths 390, 405 and 460 nm were determined. 10. Recommendations are given for the optimization of the indicator reaction in the determination of acid phosphatase by hydrolysis of naphthyl phosphate.

Acid Phosphatase↗