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PubMed1980

Comparative studies on acid phosphatase isozymes of developing human placenta and fetal liver.

Acid phosphatases from human placenta and fetal liver during ontogenic development have been studied by electrophoresis on polyacrylamide gels. Three isozymes have been detected in liver as well as in early and term placenta, and one more in placenta at mid-gestation. These isozymes behaved differentially towards heat and a number of inhibitors at different weeks of gestation. Quantitative determination of each isozyme also showed stage-specific variation.

Acid Phosphatase↗
PubMed1975

The effect of cancer chemotherapy on lysosomal enzymic activities (acid phosphatase) of Ehrlich ascites carcinoma cells.

The distribution of acid phosphatase in Ehrlich ascites carcinoma cells was studied by histochemical techniques in mice treated with antitumoral agents (Tio-Tepa, Cosmegen). The results proved the accuracy of the histoenzymatic demonstration of APh activity for the study of early changes induced in Ehrlich ascites tumor by antitumoral drugs : these changes precede those revealed by routine histological methods and are related to the degree of sensitivity of the tumor to the drugs.

Acid Phosphatase↗
PubMed1980

The simultaneous identification of seminal acid phosphatase and phosphoglucomutase by starch gel electrophoresis.

Although elevated acid phosphatase (AP) activity in vaginal fluid is a consistent indicator for semen, differentiation between vaginal AP and seminal AP provides a more meaningful result. Detection of seminal AP in mixtures of vaginal AP, feces, and blood is accomplished by starch gel electrophoresis, employing the substrate thymolphthalein monophosphate as a selective visualization agent. Genetic phosphoglucomutase isoenzymes are simultaneously separated by this method and allow differentiation in some semen/vaginal fluid mixtures.

Acid Phosphatase↗
PubMed1977

Dissociation-recombination of sunflower seed acid phosphatase.

Formal genetic studies of sunflower (Helianthus annuus) seed acid phosphatase (ACP, E.C. 3.1.3.2) had suggested that the functional enzyme consists of two polypeptide subunits. The dimeric quaternary structure was demonstrated by dissociation-recombination procedures. Dissociation of electrophoretically distinct homodimers was effected upon freezing of extracts in a pH 8-9 buffer containing 1 M NaCl and 0.1 M 2-mercaptoethanol. Reassociation, as indicated by the formation of the hybrid isozyme, occurred during 12 hr dialysis against a pH 7.0 buffer.

Acid Phosphatase↗
PubMed1975

Report and characterization of a new variant, EB, of human red cell acid phosphatase.

A new variant phenotype of human red cell acid phosphatase, designated EB, was discovered in a male during a survey of blood donors from Copenhagen, Denmark. Electrophoretically, the variant revealed the two isozymes corresponding to the B type as well as two fast moving anodic isozymes. The enzyme activity and thermostability were found to be higher than in any earlier reported type. Isoelectric focusing of the variant type indicated that the isoelectric point of the variant enzyme is lower than in the common types.

Acid Phosphatase↗
PubMed1990

Multiple forms of barley root acid phosphatase: purification and some characteristics of the major cytoplasmic isoenzyme.

The major acid phosphatase form (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) was purified from the soluble extract of barley roots. The enzyme is homogeneous on polyacrylamide gel electrophoresis and moves as a single band of Mr approximately 38,000 in the presence of sodium dodecyl sulphate. The molecular weight of the native enzyme was Mr 77,600 and 79,000 as determined, respectively, by gel filtration on a Sephadex G-100 column and by density gradient ultracentrifugation. The isoelectric point was about 6.28. The enzyme is competitively inhibited by molybdate (Ki = 9 x 10(-7) M). NaF, Ag(+), Hg(2+), Pb(2+) and Zn(2+) are also inhibitors, while other cations showed no effect. The enzyme hydrolyzes a wide variety of natural and synthetic phosphate esters. In particular, the enzyme seems to be active on ATP, o-phosphotyrosine, o-phosphoserine and glucose 1-phosphate. The pH dependence studies between pH 4-8 using p-nitrophenylphosphate as substrate and diethylpyrocarbonate inactivation indicate the presence of essential histidine residue at the active site.

Acid Phosphatase↗
PubMedDate not supplied

Further studies on acid phosphatase in obese subjects.

Low activity genetic variants of acid phosphatase (ACP1) are positively associated with extreme body mass deviations in obese subjects. The same pattern has been found in non-diabetic children, in diabetic pregnant women, and in non-diabetic adult subjects. Low activity variants of ACP1 also show a positive association with family history of obesity, supporting the hypothesis of an enhancing action of these variants on expressivity of obesity.

Acid Phosphatase↗
PubMed1995

In vivo and in vitro analysis of lysosomes and acid phosphatase activity in human chagasic placentas.

A structural, cytochemical, stereological, and biochemical study of lysosomes and a lysosome marker, the enzyme acid phosphatase, was performed, both in placentas at term from chagasic pregnant women without fetal infection and in normal placentas at term cocultured in vitro with Trypanosoma cruzi. It was found that in placentas from chagasic women lysosomes were normally distributed in the trophoblast. Stereological analysis showed that lysosomes and cytochemical acid phosphatase (AcP) activity were increased in the trophoblast of chagasic placentas. AcP activity increased in subcellular fractions of the isolated trophoblast from chagasic placentas, and the lysosomal fraction of those placentas exhibited the highest value of enzymatic activity in comparison to controls (P < 0.05). No differences in AcP activity were observed between homogenates of normal placentas cocultured with T. cruzi and controls. These data suggest that the placental lysosome population might be involved in the process of placental infection by T. cruzi.

Acid Phosphatase↗
PubMed1987

Media-induced departures from the usual, temperature-dependent cell shapes of Sporothrix schenckii and concomitant changes in the acid phosphatase isoenzyme patterns.

Sporothrix schenckii grew as mycelia at 20 degrees C or yeast at 35 degrees C on a common culture medium, YNG (yeast extract, neopeptone and glucose), in agreement with previous observations that standard media support the mycelial phase at the lower temperature and the yeast phase at the higher temperature. Special media, M-1 and M-2, were used to generate yeast at 20 degrees C and mycelia at 35 degrees C, respectively, i.e. the reverse of the typically-observed, temperature-dependent phases. In this context the M-1 induced (or forced) generation of yeast cells at 20 degrees C was judged to be abnormal yet these cells had a typical yeast ultrastructure including the definitive microfibrillar zone of the cell envelope. Electropherograms of extracts of these cells (M-1 at 20 degrees C) displayed the typical acid phosphatase isoenzyme pattern of yeast grown at 35 degrees C, and that is much more complicated than the typical pattern for extracts of mycelia grown at 20 degrees C on YNG. On the other hand the fungus was held in the mycelial phase on M-2 at 35 degrees C, at least for short term cultures, to complement the study and provide a departure from the cell shape which is expected at the higher temperature. These mycelia were judged to be ultrastructurally abnormal in that they had a thin microfibrillar zone not previously seen in S. schenckii mycelia produced on standard media at lower temperatures. The cell-free extract of these abnormal mycelia grown at 35 degrees C exhibited an isoenzyme pattern which was closer to that of yeast grown at 35 degrees C than to mycelia grown at 20 degrees C, although one isoenzyme showed intermediate electrophoretic mobility. The findings with M-2 medium at 35 degrees C were less meaningful because of the eventual conversion to yeast phase. Overall the results indicate an association between acid phosphatase isoenzyme pattern and cell shape, rather than simply an expression of the various acid phosphatases with growth temperature.

Acid Phosphatase↗
PubMed1987

Acid phosphatase levels in follicular fluids following induction of ovulation in in vitro fertilization patients.

Considerable evidence indicates that changes in acid phosphatase (AP) activity at the ovarian level play a role in the process of ovulation. In this study the concentrations of AP were determined in follicular fluids collected from follicles of 52 women at the time of laparoscopy performed in connection with an in vitro fertilization program. In each of the 52 women at least one ovum was harvested. Of the 52 ova, 28 cleaved in vitro, while in 24 ova cleavage was not seen. Levels of AP in follicular fluids of women whose ova did not cleave were significantly lower than those found in follicular fluids of women with at least one ovum undergoing cleavage: 0.45 +/- 0.14 (SE) and 4.78 +/- 0.37 Bess Lowry Units (BLU), respectively. Comparison of AP levels in follicular fluids of women who conceived (5) and women whose ova cleaved, but in whom pregnancy was not achieved (23), did not reveal significant differences: 5.87 +/- 1.29 and 4.55 +/- 0.35 BLU, respectively. Moreover, the enzyme level was typical for a woman and not for a follicle. Fluids of two different follicles of the same woman, when one ovum cleaved and one did not, showed similar AP levels. AP levels were high in all samples follicles of women in whom at least one ovum cleaved. These findings indicate that the presence of certain levels of acid phosphatase represents an important, albeit not the sole, condition for ovum maturation. Moreover, the follicular fluid levels of AP could serve as an indicator of proper timing of the follicular puncture in relation to the human chorionic gonadotropin injection (or the luteinizing hormone peak).

Acid Phosphatase↗
PubMed1990

Toxic impact of phosphamidon on acid phosphatase of prawn, Metapenaeus monoceros (Fabricius).

Activity levels of acid phosphatase (ACPase) in midgut gland and muscle tissues of penaeid prawn, Metapenaeus monoceros were studied after exposure to selected sublethal concentrations of phosphamidon after acute and chronic exposure. Phosphamidon was found to elevate the activity levels of ACPase in the selected tissues. The rate of elevation of ACPase is dose-dependant and is more at higher concentrations. Acute and chronic exposure to phosphamidon creates disturbances in the normal functioning at the cellular level in the tissues of prawn, M. monoceros.

Acid Phosphatase↗
PubMed1976

Histochemical mapping of certain enzymes in few fresh water teleosts. I. Acid phosphatase.

A detailed investigation of the distribution pattern of acid phosphatase in the different parts of alimentary canal and associated glands of Colisa fasciatus, Macrognathus aculeatus, Notopterus notopterus and Nandus nandus has been made. Though this enzyme shows its hydrolytic activity in all the parts of the digestive system yet its intense activity has been noted in the intestine, pyloric caeca, liver and pancreas of all the 4 fishes. Mucosal and submucosal layers of all the parts of the alimentary canal are the main seat of localization of this enzyme.

Acid Phosphatase↗
PubMed1989

Acid phosphatase levels in serum during transurethral prostatectomy.

Serum prostatic acid phosphatase (S-PAP), serum electrolytes, blood loss and volume of irrigating fluid absorbed were measured during 10-min periods in the course of 35 transurethral prostatic resections. Elevation of the S-PAP concentration occurred in association with a large blood loss, with absorption of irrigant followed immediately by hyponatraemia, and with a sudden drop in systolic blood pressure. The volume of blood lost during irrigant absorption was the most important index of the S-PAP level. A model for the transfer of PAP to the circulation during TURP is presented.

Acid Phosphatase↗
PubMed1999

Fluoride inhibition of bovine spleen purple acid phosphatase: characterization of a ternary enzyme-phosphate-fluoride complex as a model for the active enzyme-substrate-hydroxide complex.

Purple acid phosphatases (PAPs) employ a dinuclear Fe(3+)Fe(2+) or Fe(3+)Zn(2+) center to catalyze the hydrolysis of phosphate monoesters. The interaction of fluoride with bovine spleen purple acid phosphatase (BSPAP) has been studied using a combination of steady-state kinetics and spectroscopic methods. For FeZn-BSPAP, the nature of the inhibition changes from noncompetitive at pH 6.5 (K(i(comp)) approximately K(i(uncomp)) approximately 2 mM) to uncompetitive at pH 5.0 (K(i(uncomp)) = 0.2 mM). The inhibition constant for AlZn-BSPAP at pH 5.0 (K(i) = 3 microM) is approximately 50-70-fold lower than that observed for both FeZn-BSAP and GaZn-BSPAP, suggesting that fluoride binds to the trivalent metal. Fluoride binding to the enzyme-substrate complex was found to be remarkably slow; hence, the kinetics of fluoride binding were studied in some detail for FeZn-, AlZn-, and FeFe-BSPAP at pH 5.0 and for FeZn-BSPAP at pH 6.5. Since the enzyme kinetics studies indicated the formation of a ternary enzyme-substrate-fluoride complex, the binding of fluoride to FeZn-BSPAP was studied using optical and EPR spectroscopies, both in the presence and absence of phosphate. The characteristic optical and EPR spectra of FeZn-BSPAP. F and FeZn-BSPAP.PO(4).F are similar at pH 5.0 and pH 6.5, indicating the formation of similar fluoride complexes at both pHs. A structural model for the ternary enzyme-(substrate/phosphate)-fluoride complexes is proposed that can explain the results from both the spectroscopic and the enzyme kinetics experiments. In this model, fluoride binds to the trivalent metal replacing the water/hydroxide ligand that is essential for the hydrolysis reaction to take place, while phosphate or the phosphate ester coordinates to the divalent metal ion.

Acid Phosphatase↗
PubMed1985

Influence of seasons on circadian rhythm of acid phosphatase and beta-acetyl-glucosaminidase activity in the mouse salivary gland and liver.

Influence of seasons on circadian changes in acid phosphatase and beta-acetylglucosaminidase activity was studied in the liver and submandibular gland of sexually mature mice. Seasonal differences in circadian rhythm was found in both examined enzymes in both organs. These changes were independent from each other and each rhythm was differently subjected to seasonal changes. The lowest seasonal influence was observed in acid phosphatase in the salivary gland. Activity of the other enzymes changed in different degrees, having their acrophases at different times of the day and different rhythm intensity. The highest circadian activity changes measured by amplitude and mesor were observed in spring and summer whereas in the autumn and winter their activity had much weaker rhythms or even they disappeared completely. An attempt was made to explain the observed changes by changes in hormonal background and a certain kind of genetic memory pertaining to laboratory animals.

Acclimatization↗
PubMed1993

Acid phosphatase activity in Coxiella burnetii: a possible virulence factor.

High-speed supernatant fluids derived from sonicated Coxiella burnetii contained considerable acid phosphatase activity when assayed by using 4-methylumbelliferylphosphate; they also contained a factor that blocked superoxide anion production by human neutrophils stimulated with formyl-Met-Leu-Phe. The pH optimum of the enzyme was approximately 5.0. The level of phosphatase activity detected in several isolates of C. burnetii implicated in acute (Nine Mile) and chronic (S Q217, PRS Q177, K Q154) Q fever was 25 to 60 times greater than that reported in other microorganisms, including Leishmania and Legionella spp. The enzyme was found in rickettsiae grown in different hosts (L929 cells and embryonated eggs) and, in the case of L929 cells, for both short periods (less than a month) and the long term (years). Cytochemical techniques coupled with electron microscopy localized the phosphatase activity to the periplasmic gap in the parasite. Ion-exchange chromatography revealed a major species of the enzyme and showed that the enzyme of the parasite was distinct from that of the host cell (L929 fibroblasts); its apparent molecular weight was 74,000. Phosphatase inhibitors (i.e., molybdate heteropolyanions) had differential effects on the phosphatases of the parasite and host cell. C. burnetii supernatant fluid inhibited superoxide anion production by formyl-Met-Leu-Phe-stimulated human neutrophils; molybdate inhibitors reversed the inhibition. Treatment of C. burnetii-infected L929 cells with one of the molybdate compounds (complex B') significantly reduced the level of infection and did not affect the viability or growth of the host cell. These data suggest that the acid phosphatase of the parasite may be a major virulence determinant, allowing the agent to avoid being killed during uptake by phagocytes and subsequently in the phagolysosome.

Acid Phosphatase↗
PubMed1979

Ultracytochemical study on eccrine acrosyringium of human embryos. Acid phosphatase activity during formation of lumen.

Ultracytochemical demonstration of acid phosphatase (ACPase) activity during the developing of intraepidermal eccrine sweat duct (eccrine acrosyringium) of human embryos was performed in order to elucidate the functional relationship between multivesicular dense bodies and intracellular cavities formed within the inner cells of eccrine sweat apparatus anlagen and to clarify the ultracytochemical characteristics of the multivesicular dense bodies. ACPase activity was characteristically detected in the unit membrane structures of small pinched-off vesicles within cavities and of immature microvilli lining these cavities as well as in those of multivesicular dense bodies. These findings give strong support to the theory that the multivesicular dense bodies are lysosomes and through their action the autolytic formation of intraepidermal eccrine sweat duct is carried out.

Acid Phosphatase↗
PubMed1979

Three different acid phosphatase patterns in leukaemic lymphoid T-cells.

The acid phosphatase pattern was studied in leukaemic cells from 8 patients with T-cell leukaemia (5 ALL and 3 CLL). In 2 cases the enzyme activity was focal granular with paranuclear localization as earlier demonstrated by other authors, while--in contrast to these findings--the enzyme activity in 4 cases demonstrated universal granular distribution. Almost all the cells from each patient showed the same picture. In the last 2 cases a mixed focal and universal granular pattern was observed, where half the cells possessed the focal form and the other half the universal form of granular activity. The two first-mentioned patterns were observed in cases of T-ALL as well as of T-CLL, while the mixed pattern was seen only in cases of T-ALL.

Acid Phosphatase↗