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At least 1,387 records · Page 77Linked to original sources
PubMed2003

Quantification of tartrate resistant acid phosphatase distribution in mouse tibiae using image analysis.

Tartrate resistant acid phosphatase (TRAP) activity of bone is a suitable biochemical marker for osteoclastic bone resorption. Qualitatively, the histochemical distribution of TRAP has been used to identify osteoclasts responsible for bone resorption; however, there have been few attempts to quantify TRAP localization. We describe a method for evaluating bone resorption by quantifying area percentages of positive TRAP localization using image analysis. Mouse tibiae were paraffin embedded following demineralization in disodium ethylenediamine tetraacetic acid. Longitudinal sections of tibia were cut from 15 levels in the left and the right limbs of six mice (180 sections total) and stained for TRAP distribution. Positive TRAP localization was quantified by pixel area count and reported as a percentage of the total tissue area specified. The 1.85 mm2 region of interest was placed at the midpoint of the epiphyseal growth plate containing the provisional calcification layer and the primary spongiosa, while excluding cortical bone of each mouse tibia. The percentage of TRAP localization ranged from 0.95 to 1.31% and was not significantly different from level to level or limb to limb in each mouse (p > 0.100). Within the same region of interest, an osteoclast count along the bone perimeter also was performed. We demonstrated a strong correlation (r2 = 0.903) between the conventional histomorphometric osteoclast index and positive TRAP localization, validating the latter as an alternative method to assess bone resorption. Quantitative analysis of TRAP is significant because it allows statistical comparisons between treatment groups, promotes precise pathological diagnoses and facilitates a reference data base that may aid the study of bone related diseases involving increased bone resorption.

Acid Phosphatase↗
PubMed1984

[Plasma cell acid phosphatase in the differential diagnosis of monoclonal gammopathies].

Acid phosphatase activity was studied cytochemically in bone marrow plasma cells of 32 multiple myelomas, 45 non-myelomatous monoclonal gammopathies and 20 normal subjects. We have found significant differences among these three groups (P less than 0.001). The usefulness of this cytochemical reaction for the study of monoclonal gammopathies is discussed.

Acid Phosphatase↗
PubMed1981

Role of acid phosphatase measurement in management of prostate cancer.

Serum acid phosphatase was measured in 155 people of whom 45 had prostate cancer and 110 were either normal or had other conditions. The assay did not discover early cases of prostate cancer but did reveal accurately patients with metastatic prostate cancer. The assay appears to be valuable for the purposes of staging the disease but as a method of discovering patients with early forms of prostate cancer.

Acid Phosphatase↗
PubMed1987

Use of TnphoA to detect genes for exported proteins in Escherichia coli: identification of the plasmid-encoded gene for a periplasmic acid phosphatase.

The structural gene (appA) for the periplasmic acid phosphatase (optimum pH 2.5) of Escherichia coli was cloned into a plasmid by using a combination of in vivo and in vitro techniques. The position and orientation of the appA gene within the cloned DNA fragment were identified by using fusions to the alkaline phosphatase gene (phoA) generated by Tn5 IS50L::phoA (TnphoA) insertions. For TnphoA-generated hybrid proteins to have high enzymatic activity, it appears that the phoA gene must be fused to a target gene coding for a signal which promotes protein export. The approach used to identify the appA gene thus appears to provide a simple general means of selectively identifying genes encoding membrane and secreted proteins.

Acid Phosphatase↗
PubMed1980

Prostatic trauma and release of acid phosphatase. Radioimmunochemical and enzymatic comparison.

Radioimmunoassay for prostatic acid phosphatase and a conventional enzymatic method using alpha-naphthyl phosphate were employed to document the changes in serum levels of this enzyme following transurethral prostatectomy and prostatic massage. Thirty-four patients with histologically proved benign prostatic hyperplasia and 120 controls were studied. Consistent parallel elevations were noted after surgical trauma. A rapid clearance was observed with normal levels returning at twenty-four hours. Prostatic massage did not elicit a change by either method.

Acid Phosphatase↗
PubMed1980

Cytochemical localization of acid phosphatase and trimetaphosphatase activities in exocrine acinar cells.

Acid phosphatase activity, a lysosomal marker, is commonly demonstrated using the Gomori technique with cytidine 5'-monophosphate or beta-glycerophosphate as substrate. Using this lead capture method on mouse and rat exorbital lacrimal, parotid, and pancreatic acinar cells, reaction product was localized in GERL, forming secretory granules, and secondary lysosomes. However, a different cytochemical localization was observed for inorganic trimetaphosphatase, another lysosomal enzyme. When the technique for trimetaphosphatase activity, a metal chelation method, was applied to exocrine acinar cells, reaction produce was conspicuously absent from GERL and forming secretory granules, but was present in secondary lysosomes, occasionally in Golgi saccules, and in previously unreported basal elongated lysosomes. The differences in the localization of the two enzymatic activities emphasizes the importance of employing more than one substrate where possible, and raises questions concerning the mechanism of delivery of acid hydrolases to secondary lysosomes.

Acid Anhydride Hydrolases↗
PubMed1979

Deletion mapping: further evidence for the location of acid phosphatase (ACP1) within 2p23.

The human red cell acid phosphatase (ACP1) locus was assigned to region 2p23 leads to 2pter by Ferguson-Smith et al [3], more specifically to 2p23 by Hamerton et al [5]. We describe two unrelated patients with deletion of chromosome 2, with similar breakpoints in the distal portion of band p23 (del(2) (p23)). ACP1 typing in both patients revealed heterozygous BA phenotypes. Thus, we assign the locus for ACP1 to the distal portion of 2p23.

Abnormalities, Multiple↗
PubMed1987

An improved procedure for the X-ray microanalysis of acid phosphatase activity in lysosomes.

The useful detection of acid phosphatase activity with cerium as a capturing agent is confirmed. By introducing a freeze step in combination with a preincubation, reliably localized, lysosomal precipitates are obtained and aspecific ones prevented. Short (t less than 1 h) postfixation with either OsO4 plus K4Fe (CN)6 or OsO4 plus aminotriazole, added to lysosomal cerium localization a high membrane contrast. The detection of cerium by X-ray microanalysis is improved by a better spectral separation of the osmium (M alpha) and cerium (L alpha) peaks.

Acid Phosphatase↗
PubMed1983

Stabilization of human prostatic acid phosphatase by cross-linking with diamines.

The acid phosphatase [EC 3.1.3.2] from human prostate gland is very unstable glycoprotein. To stabilize the enzyme cross-linking reaction with diamines was adopted. The carboxyl groups of the enzyme were activated with 1-ethyl-(3-dimethylaminopropyl)-carbodiimide and then treated with diamines of H2N-(CH2)n-NH2 type. The modified enzyme with 1,12-dodecamethylenediamine preserved about 80% of its original activity and showed enhanced thermostability. Gel filtration and SDS-polyacrylamide gel electrophoresis showed the formation of cross-linked products with original molecular weight 100 KD and higher enzymatically active species.

Acid Phosphatase↗
PubMed1993

Serum acid phosphatase in TUR syndrome.

The value of serum acid phosphatase (S-ACP) as a marker of transurethral resection (TUR) syndrome was studied in 105 patients undergoing TURP. In ten patients who developed TUR syndrome the elevation of S-ACP was statistically significantly higher than in the rest of the patients. In seven patients prostatic cancer was diagnosed in the resection chips, but there were no differences in the S-ACP levels during TURP between these patients and the rest of the group. According to the present study, S-ACP seems to be a reliable and cheap marker of TUR syndrome, but the method is slow as compared to ethanol, which restricts its use.

Acid Phosphatase↗
PubMed2003

Identification of gp17 glycoprotein and characterization of prostatic acid phosphatase (PAP) and carboxypeptidase E (CPE) fragments in a human seminal plasma fraction interacting with concanavalin A.

The decapacitating fraction of human seminal plasma, which strongly interacts with concanavalin A, is constituted by high mannose-type N-linked glycoproteins, most of them of less than 44 kDa. Each component with apparent molecular mass of 30, 18, and 17 kDa respectively, as judged by SDS-PAGE, was submitted to "in gel" digestion with trypsin followed by HPLC separation of the peptides and sequencing. They were characterized at microscale as gp17, an aspartyl protease that possibly contributes to liquefaction of the seminal plasma coagulum, two fragments of human acid phosphatase (17 and 30 kDa, respectively), and a 17-kDa fragment of carboxypeptidase E. Neither the fragments of prostatic acid phosphatase nor that of carboxypeptidase E had been described before in the human seminal fluid. Very weak bands, of apparent molecular masses 44 and 52 kDa, are consistent with presence of small amounts of parent compounds, prostatic acid phosphatase and carboxypeptidase E.

Acid Phosphatase↗
PubMed2003

Concentration-dependent dissociation/association of human prostatic acid phosphatase.

The apparent molecular mass of human prostatic acid phosphatase (PAP) was estimated over a wide range of enzyme concentrations using equilibrium centrifugation in the "Airfuge" tabletop ultracentrifuge. We show that the average mass of all active PAP species steeply increases at enzyme concentrations around 100 nM. The data indicate that at lower concentrations, active monomer prevail, whereas at concentrations above 100 nM, PAP active dimers are formed. These findings were confirmed by measurements of fluorescence emission intensity as a function of enzyme concentration. A shift of the normalized PAP fluorescence intensity around 100 nM independently indicates that a major structural change of the PAP protein occurs in that range of concentrations. From these findings, we conclude that in dilute solutions, several active PAP species exist, which are involved in concentration-dependent dissociation/association equilibria.

Acid Phosphatase↗
PubMed1998

Follow-up on the Berg acid phosphatase test.

Approximately 42 years ago, the Berg acid phosphatase (AP) test (1) was accepted in most rape treatment centers nationally as the standard to determine whether sexual intercourse or related actions in any form had occurred. More specifically, the test was designed to determine the presence of a certain enzyme. In October 1969, I published an article making the test simpler (2) and reviewing the history of various tests for the detection of AP, an enzyme found in great abundance in seminal fluid. Both AP-impregnated material and refrigerated reagents had been saved along with a quantity of seminal fluid used in the original tests. The objectives of this study were to determine whether 25-year-old seminal fluid in any form can still be identified by the AP test and whether 25-year-old chemicals have remained stable and are still usable.

Acid Phosphatase↗
PubMed1980

The radioimmunochemical measurement of prostatic acid phosphatase: current state of the art.

A novel radioimmunochemical method for the measurement of human prostatic acid phosphatase in serum and bone marrow has demonstrated distinct biochemical advantages over the standard enzymatic techniques that are currently utilized in the clinical laboratory. The promising nature of the immunochemical assay now in clinical assessment for prostatic cancer may lend itself particularly to more sensitive confirmation of the presence of prostatic neoplasia as well as significantly more precision in the clinical staging of the disease process. In its present form, utilization of the technique as a reliable screening test for early prostatic cancer is patently inappropriate from a biochemical and biostatistical point of view. Continuing research on the antigenic nature of the human prostatic acid phosphatase molecule and the development of antibody with enhanced specificity may somewhat resolve the current screening problem. However, the essentially insoluble problem of the relatively low prevalence rate for prostatic cancer in males in the United States will persist and will probably limit the clinical application of enzymatic and radioimmunochemical screening techniques for early prostatic cancer.

Acid Phosphatase↗
PubMed1984

Enzymatically active zinc, copper and mercury derivatives of the one-iron form of pig allantoic fluid acid phosphatase.

Derivatives of the violet, iron-containing acid phosphatase of pig allantoic fluid have been prepared in which one of the two iron atoms present in the native enzyme has been replaced by zinc, copper or mercury. The derivatives so formed are enzymatically active: the Zn-Fe, Cu-Fe and Hg-Fe enzymes have specific activities of about 80%, 25% and 17% respectively, of the maximum specific activity of the Fe-Fe enzyme in the standard assay at pH 4.9 with p-nitrophenyl phosphate as substrate. In contrast to the Fe-Fe enzyme, the mixed metal derivatives are not rapidly inactivated by H2O2. Visible absorption spectra of the derivatives confirm that all of the visible absorption of the Fe-Fe enzyme is due to one of the iron atoms. Attempts to prepare an active Cu-Cu enzyme were unsuccessful.

Acid Phosphatase↗
PubMed2000

Deletion of the gene for the membrane-bound acid phosphatase of Leishmania mexicana.

The membrane-bound acid phosphatase of Leishmania mexicana (LmxMBAP) has been shown to be a heterogeneously N-glycosylated type I transmembrane protein, which is localized predominantly in vesicular structures close to the flagellar pocket in promastigotes and amastigotes. Its expression in both life stages prompted us to analyse its function by performing deletion analysis. Both alleles of the single copy gene were sequentially replaced by resistance marker genes and the resulting deletion mutant was tested for its potential to infect Balb/c mice and peritoneal macrophages. There was no obvious difference detectable between the mutant and the wild-type. Therefore, we conclude that LmxMBAP is neither involved in the infection process nor required for amastigote survival in the infected host cell. LmxMBAP null mutant promastigotes were used to establish a system for homogeneous overexpression of LmxMBAP which will be useful to investigate protein sorting in L. mexicana.

Acid Phosphatase↗
PubMed1991

Stabilization of human prostatic acid phosphatase by coupling with chondroitin sulfate.

Human prostatic acid phosphatase (PAP) (EC 3.1.3.2) was covalently linked to chondroitin sulfate A from whale cartilage. In order to bind the protein amino groups with the preactivated carboxyl groups of chondroitin sulfate, 1-ethyl-3-(3'-dimethylaminepropyl)carbodiimide and N-hydroxysulfosuccinimide were used as coupling agents. The product was soluble and enzymatically active. The activity was on average 25% higher than that of the free enzyme. The product was heterogeneous in respect to charge and Mr (50-1500) kDa, as determined by chromatography on Sephacryl S 300 and polyacrylamide gel electrophoresis. The resulting polymers contained covalently bound chondroitin sulfate, as shown by the biotin-avidin test. The modified enzyme is more resistant against various denaturing agents, e.g., urea, ethanol, and heat. Thus covalent modification of PAP by cross-linking to chondroitin sulfate could be the preferred method for stabilization of its biological activity.

Acid Phosphatase↗