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PubMed1977

Allergens in bee venom. III. Identification of allergen B of bee venom as an acid phosphatase.

Allergen B previously isolated from honeybee venom and shown to be a mildly acidic protein consisting of polymers of a chain of 49,000 d is shown to have acid phosphatase activity. Allergen B is homogeneous by several criteria. No acid phosphatase, alkaline phosphatase, or esterase activity was found in any other allergen or fraction of bee venom. Acid phosphatase activity was also found in yellow jacket venom and extracts of venom sacs from bumblebees and paper wasps.

Acid Phosphatase↗
PubMed2000

Purification and properties of an acid phosphatase from Entamoeba histolytica HM-1:IMSS.

Entamoeba histolytica contains and secretes acid phosphatase, which has been proposed as a virulence factor in some pathogenic microorganisms. In this work, we purified and characterised a membrane-bound acid phosphatase (MAP) from E. histolytica HM-1:IMSS and studied the effect of different chemical compounds on the secreted acid phosphatase and MAP activities. MAP purification was accomplished by detergent solubilisation, and affinity and ion exchange chromatographies. The enzyme showed a pI of 5.5-6.2, an optimum pH of 5.5, and a Km value of 1.14 mM with p-nitrophenyl phosphate.

Acid Phosphatase↗
PubMed1982

Quantitative x-ray microanalysis of spleen lysosomes after acid phosphatase reaction.

A quantitative X-ray microanalytical study of 80 spleen lysosomes after histochemical reaction for acid phosphatase was carried out. Lysosomal Fe concentrations showed a skewed distribution, with most lysosomes having relatively low concentrations. The concentration of Pb in the lysosomes (indicative of acid phosphatase activity) showed a close to normal distribution. Although the plot of lysosomal Pb concentrations against Fe concentrations showed a marked scattering of the points, there is a statistically highly significant correlation between accumulated metal and acid phosphatase activity as determined from the Pb concentrations. The relation between concentrations of P and those of Pb in the lysosomes points to the possibility that Pb(H2PO4)2 is the main reaction product of the histochemical acid phosphatase reaction.

Acid Phosphatase↗
PubMed1989

On the acid phosphatase isoenzymes existing in American Leishmania promastigotes.

1. Two partially purified acid phosphatase activities present in American Leishmania promastigote homogenates were characterized by biochemical methods. 2. One isoenzyme acts preferentially on p-nitrophenyl phosphate, is strongly inhibited by 30 mM alloxan, citrate, maleate, malonate and succinate, and strongly stimulated by 3 mM spermine. Its pI is 4.8. 3. The other isoenzyme acts preferentially on beta-glycerophosphate and is resistant to 30 mM alloxan, citrate, maleate, malonate and succinate and also to 3 mM spermine. Its pI is 5.7. 4. Both acid phosphatase isoenzymes have an optimum pH of 5.2, are tartrate-sensitive and strongly membrane-bound, as shown by differential centrifugation and density gradient equilibration. 5. Both isoenzymes were separated by using homogenates prepared in 2% Triton X-100, differential centrifugation, Sepharose 4B/CL-4B gel filtration, ion exchange chromatography and electrofocusing. After this procedure, they were still contaminated with several different proteins. 6. Purification was around 150-fold, with a 32% yield. 7. When these acid phosphatase activities were measured in total homogenates from 12 different Leishmania isolates, p-nitrophenyl phosphatase specific activity values were quite close; beta-glycerophosphatase-specific activity had around a 2-fold variation. 8. This variation was independent from taxonomic classification or infectivity of susceptible hosts.

Acid Phosphatase↗
PubMed1990

Lipophosphoglycan and secreted acid phosphatase of Leishmania tropica share species-specific epitopes.

Several species-specific monoclonal antibodies (T11, T13-T15) which only react with Leishmania tropica, recognize phosphorlated carbohydrate epitopes on lipophosphoglycan and the structurally related molecule, phosphoglycan, which is shed by promastigotes into spent culture medium. During immunoaffinity isolation of [32P]orthophosphate-labeled phosphoglycan on monoclonal antibody T15 conjugated to Sepharose 4B, a high-Mr component (approx. 200,000) was co-purified. The latter material is metabolically labeled with [35S]methionine and [3H]glucosamine. This glycoprotein was separated from phosphoglycan by chromatography on lentil lectin resin. The glycoprotein exhibited a L-tatrate-sensitive acid phosphatase activity, typical of secreted acid phosphatase (EC 3.1.3.2) from Leishmania. Monospecific antibodies to Leishmania donovani-secreted acid phosphatase selectively precipitated the L. tropica enzyme from immunoaffinity purified mixtures of the two antigens, and monoclonal antibodies to lipophosphoglycan precipitate the pure enzyme. Species-specific monoclonal antibodies to L. major lipophosphoglycan also recognized both L. tropica antigens. Treatment of the acid phosphatase with periodate or phosphodiesterase I abolished binding by the monoclonal antibodies to the pure enzyme. These results demonstrate that the two major secreted glycoconjugates of Leishmania tropica, the lipophosphoglycan and the acid phosphatase, share species-specific phosphorylated carbohydrate epitope(s).

Acid Phosphatase↗
PubMed1980

Ultrastructural localization of acid phosphatase in denervated and diabetic striated muscles.

Catabolism in denervated and diabetic rat skeletal muscle undergoing accelerated protein degradation has been investigated with methods for demonstrating acid phosphatase ultrastructurally. Control muscles displayed strong acid phosphatase activity in lateral sacs and in sparse secondary hysosomes distributed mainly near nuclear poles. Muscles from diabetic rats and, to a lesser extent, 2-day denervated rats, revealed increased secondary lysosomes apparently derived from fusion of mitochondria with acid-phosphatase-reactive vesicles and cisternae. The latter were interpreted as possibly originating from T tubules. Reaction product was also noted in the junctional folds of the motor end plate of a denervated muscle. At the longer post denervation intervals studied, deposits indicative of acid phosphatase were dispersed throughout the sarcoplasm with greater concentration in the I band and appeared more abundant in denervated than in contralateral control muscles. The enzymatic basis for the sarcoplasmic deposits and other deposits was confirmed by their absence from cytochemical controls, which included incubation in substrate-free medium, heat or NaF inactivation of enzyme, and exposure sequentially to PbNO3 and NaH2PO or PbNO3 and beta-glycerophosphate.

Acid Phosphatase↗
PubMed1986

Demonstration of tartrate-resistant acid phosphatase in un-decalcified, glycolmethacrylate-embedded mouse bone: a possible marker for (pre)osteoclast identification.

Fixed, undecalcified mouse long bones were embedded in glycol methacrylate (GMA), sectioned, and incubated for acid phosphatase in the presence or absence of tartrate, to investigate the feasibility of tartrate-resistant acid phosphatase as a histochemical marker for osteoclast identification. Naphthol AS-BI phosphate was used as the substrate and hexazonium pararosanaline as coupler. Cytocentrifuge preparations of mouse, rat, and quail bone marrow or frozen and GMA sections of mouse splenic tissue were used as controls to specify acid phosphatase activity. After adequate fixation, acid phosphatase activity sensitive to tartrate inhibition (TS-AP) was demonstrated in macrophages from spleen, bone marrow, and loose connective tissue surrounding bone rudiments. Acid phosphatase activity resistant to tartrate inhibition (TR-AP), was detected in multi-nuclear osteoclasts and in some mononuclear cells from bone marrow and periosteum. In cytocentrifuge preparations and frozen sections of mouse spleen, TR-AP was demonstrated after simultaneous incubation with substrate and tartrate. In GMA sections, however, TR-AP could only be demonstrated after pre-incubation with tartrate before application of substrate. We suggest that histochemical demonstration of TR-AP versus TS-AP on GMA-embedded bone sections by means of a pre-incubation method can be used as an identification marker of (pre)osteoclasts. Plastic embedding is recommended for its excellent preservation of morphology and enzyme activity.

Acid Phosphatase↗
PubMed1979

A technique for quantitating enzyme histochemistry in adjuvant arthritic joints. II. Acid phosphatase.

This paper reports on the incorporation of acid phosphatase histochemistry with a quantitative technique designed to measure the percentage of histochemically-localized enzyme-reactive cells found in adjuvant arthritic articular cartilage, synovial membrane and bone marrow. With the data presented and the comparisons made, this incorporation is validated and adjuvant arthritic acid phosphatase "lesions" established. In addition to discussing the importance of the histochemical data and its relationship with intra-articular lysosomes, the applicability of the reactive cell values to drug inhibition studies is discussed.

Acid Phosphatase↗
PubMed1982

Identification and partial characterization of an extracellular acid phosphatase activity of Leishmania donovani promastigotes.

An extracellular acid phosphatase was detected in the growth media of Leishmania donovani promastigotes. The enzyme was released at all stages of the growth cycle and in amounts which accounted for 90% of the total amount of this enzyme in the culture. The exoenzyme exhibited a pH optimum of 4.5 to 5.0 and was active with a variety of organic phosphates. The enzymatic activity was excluded from Sephacryl S-300 and was retained by ultrafilters with nominal molecular weight cutoffs of up to 300,000. The results of comparative studies indicated that the extracellular enzyme was distinct from a surface membrane-bound acid phosphatase of L. donovani promastigotes which has been previously described.

Acid Phosphatase↗
PubMed1976

Ultrastructural localization of acid phosphatase in normal and X-irradiated epidermis.

Acid phosphatase activity has been studied in normal and X-irradiated rat epidermis. A remarkable reaction increment was found in irradiated epithelium at the granular layer keeping the same pattern of distribution observed in the normal tissue. No reactive lysosomes or keratinosomes were observed in the cytochemical sections, while many keratinosomes but no lysosomes appeared in the electron microscopic preparations of irradiated animals. Irradiated epithelium is discussed as a suitable model to analyze the role of acid phosphatase in the keratinization mechanisms.

Acid Phosphatase↗
PubMedDate not supplied

Acid phosphatase distribution and localization in the fungus Humicola lutea.

Acid phosphatase activities in a culture liquid and mycelial extract were studied in submerged cultures of the filamentous fungus Humicola lutea 120-5 in casein-containingmedia with and without inorganic phosphate (Pi). The Pi-repressible influence on the phosphatase formation was demonstrated. Significant changes in the distribution of acid phosphatase between the mycelial extract and culture liquid were observed at the transition of the strain from exponential to stationary phase. Some differences in the cytochemical localization of phosphatase in dependence of Pi in the media and the role of the enzyme in the release of available phosphorus from the phosphoprotein casein for fungal growth were discussed.

Acid Phosphatase↗
PubMed1979

[Distribution of acid phosphatase in the chicken blastoderm].

The distribution of acid phosphatase in the chick blastoderm (stages 2--4 by HH) has been studied using cytochemistry. A marked increase of enzymatic activity all over the blastoderm was shown to coincide with the beginning of primitive streak formation. A part of the cells after their immigration are characterized by the fall of acid phosphatase activity. The percentage of such cells increases in the cranio-caudal direction of the definitive primitive streak. The patterns of yolk utilization upon the separation of individual embryonic rudiments are discussed.

Acid Phosphatase↗
PubMed1977

Elevated bone marrow acid phosphatase: the problem of false positives.

Bone marrow acid phosphatase values were studied in 24 patients (12 men and 12 women) selected at random, including 6 at autopsy. False positive results were noted in 8 of the 18 patients who were alive and in all 6 patients studied at autopsy. The possible causes for these falsely elevated results are discussed. The bone marrow acid phosphatase is a test of poor specificity and should not be used as the sole test on which vital decisions regarding management of the patient are based.

Acid Phosphatase↗
PubMed1981

Acid phosphatase staining pattern as an indicator of T-cell acute leukemia.

Acid phosphatase staining pattern has been variably advocated and discouraged as an indicator of T-cell differentiation of acute lymphoblastic leukemias. This study indicates that acid phosphatase staining pattern will correlate with the results of E rosette testing in both T-cell and non-T, non-B acute lymphoblastic leukemias in over 90% of cases. Acid phosphatase staining pattern may reliably be used to indicate T-cell differentiation in acute lymphoblastic leukemia in cases where insufficient material for E rosette testing is available.

Acid Phosphatase↗
PubMed1980

Immunological and biochemical evidence for identity of tartrate-resistant isoenzymes of acid phosphatases from human serum and tissues.

We purified acid phosphatase isoenzyme 5b from a human spleen affected by leukemic reticuloendotheliosis and used it to produce a specific antiserum. The antiserum was used to show complete immunological identity among isoenzymes 5a and 5b in human serum, and 5b isolated from a giant-cell bone tumor and from the spleen of a case of Hodgkin's disease. Acid phosphatase 5b in a giant-cell bone tumor was isolated for biochemical characterization. Its pH optimum and substrate specificity were very similar to those of isoenzyme 5b from human spleen.

Acid Phosphatase↗
PubMed1992

[PHO2 and GCN4 transcription activators in the regulation of Saccharomyces cerevisiae acid phosphatase synthesis].

The possibility of substitution of the PHO2 activator protein by GCN4 protein in transcriptional regulation of acid phosphatase genes PHO5 and PHO11 was demonstrated in the yeast Saccharomyces cerevisiae. We observed the increase in acid phosphatase synthesis in the case of gcn4-delta 1 pho2-delta 1 mutant transformed with YCp88 (GCN4-wt) plasmid in comparison with that in nontransformed cells. The mode of repression of acid phosphatase synthesis in two types of transformants gcn4-delta 1 pho2-delta 1 (GCN4-wt) and gcn4-delta 1 pho2-delta 1 (PHO2-wt) was studied. It wat demonstrated that repression of acid phosphatase synthesis in the first type of transformants took place at lower concentration of Pi than was necessary for the second type of transformants. The model of interactions between the GCN4 activator protein and PHO regulatory factors is proposed.

Acid Phosphatase↗
PubMed1976

Characterization of acid phosphatase isoenzymes in human skin fibroblasts.

The multiple acid phosphatase isoenzymes of cultivated skin fibroblasts were investigated in an effort to further clarify the basis of the observed molecular heterogeneity. Treatment with neuraminidase did not alter the migration of isoenzymes present prior to treatment with neuraminidase did not alter the migration of isoenzymes present prior to treatment, but additional isoenzymes were detectable after treatment. Variation of enzymes, permitting prediction of net charge and molecular size differences. Isoelectric focusing between pH 5.0 and pH 8.0 demonstrated three isoenzymes of acid phosphatase in the total cell homogenate and in the lysosomal fraction, two of which appeared to have similar isoelectric points.

Acid Phosphatase↗