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PubMed1982

[Separation and properties of multiple forms of acid phosphatase from the tissues and organs of the mulberry silkworm].

The multiple forms of acid phosphatase from the hemolymph, fat body, intestinal wall and silk gland of the silkworm larvae differing in their mobility during polyacrylamide gel electrophoresis were separated by isoelectrofocusing, gel filtration and ion-exchange chromatography and characterized in terms of their molecular weight, isoelectric points and substrate specificity. It was found that silkworm tissues contain several enzyme forms possessing broad substrate specificity (EC 3.1.3.2) as well as forms predominantly catalyzing the hydrolysis of glucose-1-phosphate (EC 3.1.3.10). The enzyme forms with a broad substrate specificity were detected in all tissues studied with the exception of hemolymph and were found to have the molecular weights above 60,000, pI greater than pH 6.0 and the highest activity within the pH range of 3.0-4.5. The enzyme forms causing predominant hydrolysis of glucose-1-phosphate detected in the hemolymph, fat body and intestinal wall are characterized by Mr = 30,000-100,000, pI below 6.0 and the highest activity within the pH range of 4.8-5.6. A possible role of the multiple forms of acid phosphatase in silkworm metabolism is discussed.

Acid Phosphatase↗
PubMed2005

Human tartrate-resistant acid phosphatase becomes an effective ATPase upon proteolytic activation.

Proteolytic cleavage in an exposed loop of human tartrate-resistant acid phosphatase (TRAcP) with trypsin leads to a significant increase in activity. At each pH value between 3.25 and 8.0 the cleaved enzyme is more active. Substrate specificity is also influenced by proteolysis. Only the cleaved form is able to hydrolyze unactivated substrates efficiently, and at pH >6 cleaved TRAcP acquires a marked preference for ATP. The cleaved enzyme also has altered sensitivity to inhibitors. Interestingly, the magnitude and mode of inhibition by fluoride depends not only on the proteolytic state but also pH. The combined kinetic data imply a role of the loop residue D158 in catalysis in the cleaved enzyme. Notably, at low pH this residue may act as a proton donor for the leaving group. In this respect the mechanism of cleaved TRAcP resembles that of sweet potato purple acid phosphatase.

Acid Phosphatase↗
PubMed1987

The "manganese(III)-containing" purple acid phosphatase from sweet potatoes is an iron enzyme.

An improved purification of the purple acid phosphatase from sweet potatoes has been developed, and the properties of the enzyme have been reexamined. Contrary to previous reports, (e.g., Y. Sugiura, et al., J. Biol. Chem., 256, 10664-10670 (1981) ), the enzyme contains two moles of iron and insignificant amounts of manganese. The specific activity of the iron-containing preparations is ca. 14 times higher than that reported previously for the purported "Mn(III)" enzyme. The sweet potato purple acid phosphatase does indeed bind manganese, but it can be removed by dialysis with no changes in specific activity or spectral properties.

Acid Phosphatase↗
PubMed1980

Sex and acid phosphatase in childhood non-T lymphoblastic leukaemia.

A semiquantitative assessment of blast cell acid phosphatase activity, expressed as a score, was made in 41 unselected children with newly diagnosed and untreated non-T acute lymphoblastic leukaemia (ALL). Despite a wide range of enzyme activity in both sexes boys had significantly higher scores than girls, and, in view of the known association between males and T ALL on the one hand, and between acid phosphatase and T ALL on the other, these findings raise the possibility that boys may have a predisposition to a type of pre-T ALL which could contribute to the as yet unexplained difference in prognosis between the sexes.

Acid Phosphatase↗
PubMed1987

Comparison of purified acid phosphatase allozymes in Drosophila virilis: differences in carbohydrate content and composition of the allozymes.

Three acid phosphatase (EC 3.1.3.2) allozymes (ACPH1, ACPH2, and ACPH4) of Drosophila virilis show different activities as measured by electrophoretic techniques. Recently, it was suggested that these differences are attributable to the variable ability of the allozymes to be incorporated into lysosomes (Narise, S., Genet. Res. Cambr., 45:143, 1985). Immunoelectrophoresis demonstrated that the activity differences between these electrophoretic variants coincided with differences in the amount of the enzyme protein in soluble fractions but not in whole cell-free extracts. These results support the idea that acid phosphatase allozymes in D. virilis are cell-localization variants. We examined the problem by structural analysis of both the protein and the carbohydrate moieties of these allozyme glycoproteins, since lysosomal enzymes are known to become localized in lysosomes through their carbohydrate moieties. The three ACPH allozymes were purified to homogeneity from their respective homozygotes and compared with respect to amino acid composition and carbohydrate content and composition. Amino acid compositions were similar, while content and compositions of neutral sugars were significantly different. The neutral sugar content of ACPH1 was 9.2%; that of ACPH2, 21.0%; and that of ACPH4, 7.3%. A trace of hexosamines, but no N-acetylneuraminic acid, was found in the ACPH allozymes. Isoelectric points varied corresponding to their electrophoretic mobilities, which were not changed by treatment with alkaline phosphatase and neuraminidase.

Acid Phosphatase↗
PubMed2001

[Development for the determination of band 5b tartrate-resistant acid phosphatase activity in serum].

Band 5 Tartrate-resistant acid phosphatase(TRACP; EC 3.1.3.2) consists of two isoenzymes, bands 5a and 5b, of which band 5b TRACP, an enzyme expressed in bone-resorbing osteoclasts, is secreted into the circulation during bone resorption. Band 5b TRACP was measured kinetically in serum as tartrate-resistant fluoride-sensitive heparin-resistant ACP with 2,6-dichloro-4-acetylphenyl phosphate as substrate at pH6.6. The within-run(n = 20) and between-run(n = 20) CVs of band 5b TRACP activity were 3.3-5.8% and 5.0-7.3%, respectively. The reference range of band 5b TRACP activity in males(n = 72) and females(n = 87) 20-39 years of age by this method were 3.7-12.5 U/l and 2.7-9.9 U/l, respectively. The band 5b TRACP value was significantly higher in post-menopausal women compared with the menstruating women. The relationship of band 5b TRACP and ultrasound findings in healthy women aged 31-75 years(n = 139) were inversely correlated with stiffness(r = -0.401), speed of sound(SOS; r = -0.386) and broadband ultrasound attenuation(BUA; r = -0.338). These results suggest that band 5b TRACP may be a useful in the evaluation of bone turnover.

Acid Phosphatase↗
PubMed1995

Ser/Thr-rich repetitive motifs as targets for phosphoglycan modifications in Leishmania mexicana secreted acid phosphatase.

The insect stage of the protozoan parasite Leishmania mexicana secretes a phosphomonoesterase in the form of a filamentous complex. The polypeptide subunits of this polymer are modified by phosphoglycans and/or oligomannosyl residues linked to phosphoserine. Based on peptide sequence data of a predominant 100 kDa protein of the filamentous complex, two tandemly arranged, single copy genes, lmsap1 and lmsap2, were cloned and sequenced. lmsap1 predicts a protein with features characteristic of acid phosphatases and a remarkable serine- and threonine-rich region of 32 amino acids close to the C-terminus. In the otherwise identical lmsap2 product, this region is extended to 383 amino acids and is composed of short Ser/Thr-rich repeats. Deletion analysis demonstrates that lmsap1 encodes the major 100 kDa protein of the complex while a minor 200 kDa component is derived from the lmsap2 gene. Null mutants of either gene retain the ability to secrete acid phosphatase filaments, while a deletion of both genes results in Leishmania defective in enzyme formation. The Ser/Thr-rich domains are the targets for phosphoglycan modifications as shown by the expression of secreted fusion proteins composed of these C-terminal regions and the N-terminal domain of a lysosomal acid phosphatase.

Acid Phosphatase↗
PubMed1982

Development and clinical evaluation of two immunoassays for prostatic acid phosphatase in serum.

Polystyrene tubes were coated with IgG, isolated from antiserum against human prostatic acid phosphatase, and incubated with a known amount of purified antigen as a standard, and sera from patients. The amount of bound prostatic acid phosphatase was established by using its enzyme activity. This was performed either spectrophotometrically with p-nitrophenylphosphate (enzyme immunoassay) or fluorometrically with alpha-naphthylphosphate as a substrate (immunofluorescence assay). Results of both methods were compared with those of the conventional method and were evaluated in four groups of patients with: non-prostatic disease, hypertrophy, treated and untreated prostatic carcinoma. The first group was used to establish the upper limit of normal. In the hypertrophy group, the specificity of the immunological methods when compared with the conventional method, improved from 79% to 91%. Sensitivity, calculated from the untreated prostatic carcinoma group, was 74% for the enzyme immunoassay (EIA) and 71% for the immunofluorescence assay (IFA). The probability of having either carcinoma or hypertrophy, given observed EIA or IFA values, was calculated by the statistical method of the logistic regression.

Acid Phosphatase↗
PubMed1975

Steady state kinetics and effect of SH inhibitors on acid phosphatase from bovine brain.

1. Product inhibition studies and transphosphorylation to methanol using two different substrates indicate that acid phosphatase from bovine brain forms a phosphoryl enzyme and that the phosphorylation step can not be rate limiting. 2. Acid phosphatase from bovine brain is inhibited by 5,5'-dithiobis-(2-nitrobenzoic acid); this inhibition can be counteracted by inorganic phosphate. Incubation of the enzyme with p-nitrophenyl phosphate in the presence of p-chloromercuribenzoate leads, initially, to a higher degree of inhibition than that found with the same concentration of inhibitor in the absence of substrate. Both the titration by 5,5'-dithiobis-(2-nitrobenzoic acid) and inhibition by p-chloromercuribenzoate are consistant with the presence of 2 SH groups per mol of enzyme.

Acid Phosphatase↗
PubMed1998

Lipid mobilization and acid phosphatase activity in lytic compartments during conidium dormancy and appressorium formation of Colletotrichum graminicola.

Colletotrichum graminicola, a pathogen of sorghum and corn, was investigated prior and during germination as to certain aspects of acid phosphatase activity and lipid mobilization. Ungerminated conidia cytoplasm was filled with lipid deposits, which were mobilized during the germination process. Cytochemical ultrastructural examination showed that conidia vacuoles exhibit acid phosphatase activity, which is suggestive of lytic activity. Lipid bodies, stored in the ungerminated conidia cytoplasm, were internalized by vacuoles in a process analogous to microautophagy and were apparently digested inside them. The lipid bodies disappeared and vacuoles became enlarged in conidial cells during germination. Appressoria also showed acid phosphatase activity in multiple heterogeneous vesicles which were, in most cases, juxtaposed with lipid bodies. These results suggest that the vacuolar system plays an important role during C. graminicola germination and that the initial stages of lipid metabolization are taking place inside the vacuoles.

Acid Phosphatase↗
PubMed1979

A histochemical study of alkaline and acid phosphatase activity in osteoarthritic synovial membrane.

In order to determine the localization and activity of alkaline and acid phosphatase in the synovial membrane of osteoarthritic hip joints, enzymo-histochemical analyses were performed using Burstone's and Barka & Anderson's methods. Frozen sections of synovial biopsy material from 12 osteoarthritic and 6 control hip joints were studied. Alkaline phosphatase was found located in fibroblasts below the lining cells and in capillaries and precapillary arterioles. Acid phosphatase was seen in the lysosomes in the lining cells. Semiquantitative evaluation by means of initial time determination showed significantly greater activity in osteoarthritic synovia than in the control group. Whilst the increased activity of lysosomal enzymes is presumably implicated in the joint cartilage damage seen in osteoarthritis, the significance of elevated alkaline phosphatase levels is not yet clear.

Acid Phosphatase↗
PubMed1986

Comparison of extracellular acid phosphatases from various isolates of Leishmania.

Forty isolates of Leishmania, representing all major species infecting humans and one parasite of lizards, were examined for their ability to secrete an extracellular acid phosphatase activity. This enzyme, which was originally described and characterized from a Sudanese strain of L. donovani, was detected in the culture supernatants of all species of promastigotes examined except for L. major and L. tarentolae. There were quantitative differences among species in their levels of enzyme activity and in the sensitivity of the exoenzyme to inhibition by L(+) tartrate. Upon electrophoresis in nondenaturing polyacrylamide gels, extracellular acid phosphatase from L. braziliensis panamensis, L. tropica, and L. mexicana showed distinctive patterns which were similar for all isolates of a given species, while enzymes from L. donovani isolates differed from one another in relative electrophoretic mobility. Enzymes from all species appeared heterogeneous, showing either discrete multiple bands or single diffuse bands on gels stained for enzyme activity. Although the biological function of the extracellular acid phosphatase is presently unknown, the exoenzyme may be of value as a diagnostic or taxonomic characteristic.

Acid Phosphatase↗
PubMed1997

Characterization of monoclonal antibodies specific to human tartrate-resistant acid phosphatase.

A major product of osteoclasts, tartrate-resistant acid phosphatase (TRAP) is an essential but insufficient enzyme for bone resorption. TRAP is an excellent cell marker for osteoclasts and macrophages and is being investigated as a serum marker for osteoclast activity in diseases of bone destruction. For decades, TRAP has also been used as a marker for hairy cell leukemia. Immunoassays for TRAP are sought to increase the sensitivity and specificity of the TRAP test for bone and hairy cells. Our laboratory recently developed a monoclonal antibody to TRAP (9C5) useful for immunohistochemical identification of TRAP-positive cells in paraffin sections. Herein, we characterize 9C5 in greater detail and report production of another anti-TRAP monoclonal antibody antibody (14G6) reactive with native, active enzyme antigen. Enzyme immunoassay, immunoprecipitation, western blot, and immunohistochemical analyses revealed the contrasting properties of 9C5 and 14G6. Antibody 9C5 reacts with a heat-denatured epitope and is suitable for denaturing western blot analysis and for immunohistochemistry. Antibody 14G6 reacts with a conformational determinant destroyed by heat and is suitable for immunoprecipitation of active TRAP, although 20% to 30% of activity is inhibited in the immune complexes. Having characterized several properties of these anti-TRAP antibodies, 9C5 and 14G6 may be useful for development of TRAP-specific immunoassays in bone pathology and hematology. They will certainly be of use for the study of biosynthesis, regulation, expression, and function of TRAP.

Acid Phosphatase↗
PubMed1980

Properties of low-molecular-weight acid phosphatases isolated from cytosol and chromatin of rat liver.

1. Acid phosphatases (orthophosphoric-monoester phosphohydrolases, acid optimum, EC 3.1.3.2) of low molecular weight were isolated from cytosol and chromatin of rat liver cells. The cytosolic enzyme was homogeneous on SDS-polyacrylamide-gel electrophoresis at pH 8.3 (mol. wt. 16 000+/-3000). Both enzymes showed similar electrophoretic mobility and molecular weight but they differed in substrate specificity, response to inhibitors and susceptibility to SH-protecting reagents.

Acid Phosphatase↗
PubMed1975

[Comparative histochemical and disc-electrophoretical investigations about the postnatal differentiation of the alkaline and acid phosphatases in the intestinal mucosa of the rat (author's transl)].

The alkaline and acid phosphatase were studied with different histochemical methods in 5 different regions of the small intestine in newborn (1. to 50. postnatal day) and in adult rats (4 month old) and compared with the results of the disk-electrophoretical fractionation of these enzymes. In the course of the adaptation of the enzymes pattern of newborn animals to the pattern of adult animals during the 3. postnatal week, in the disk-elektrophoresis there is a alteration of the qualitative composition of the enzymes. Until the 20. day the electrophoresis shows only one fraction of alkaline and acid phosphatase in duodenum. After this day three fractions can be separated. Simultaneously there is a precipitous decrease in the enzyme activities in the electropherograms of the ileum. Synchronous with the enzyme adaptation the characteristic surface epithelium of ileum is replaced by non vacuolised cylindrical epithelium.

Acid Phosphatase↗