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PubMed1977

Quantitation of vaginal acid phosphatase and its relationship to time of coitus.

In cases of alleged sexual assault a quantitative vaginal acid phosphatase determination may indicate not only the presence of seminal fluid but also the approximate time of coitus, even in the absence of spermatozoa. A method of obtaining and handling vaginal swabs allowing for acid phosphatase determination and examination for spermatozoa was developed. Postcoital samples were obtained from 26 women and analyzed for ACP activity. Quantitative levels of ACP were related to time since coitus. These levels were compared with those found in 104 cases of alleged sexual assault and in 27 women volunteers.

Acid Phosphatase↗
PubMed1980

Myeloma bone marrow acid phosphatase staining: a correlative study of 38 patients.

Acid phosphatase (AP) activity of plasma cells was studied in 38 patients with multiple myeloma (MM). The average activity per cell was strong (mean score = 2.42; maximum score = 4) and the percentage of positive cells was greater than 90% in over 71% of patients. The average AP activity per cell was higher prior to treatment (3.06 +/- 0.53) compared to relapse (2.48 +/- 0.77) and remission (1.81 +/- 1.02 (p less than 0.05 and p less than 0.01, respectively). In correlation of AP activity with clinical features at the time of the study, the only significant difference was between kappa and lambda subtype. Patients with lambda MM had a higher average AP activity per cell in remission (2.71 +/- 0.43) as opposed to kappa MM (1.17 +/- 1.06, p less than 0.05 for difference). AP activity was not significantly correlated with degree of bone involvement. However, activity seemed to be a good marker of disease activity.

Acid Phosphatase↗
PubMed1976

Trace elements and immunologic defects. Zinc deficiency and activity of lysosomal acid phosphatase in lymphocyte of mice.

Activity of lysosomal acid phosphatase in peripheral blood lymphocytes of mice fed a low-Zn diet has been studied. The study comprised 40 CBA T6T6 mice, female, aged 8 weeks, with body weight equal to about 18.0 g. The animals were fed during 10 days with a low-Zn diet. This latter diet, as well as the control one contained 0.8 mg% and 11.4 mg% of zinc, respectively; potable water contained 0.06 mg% of this element. Activity of the enzyme was determined semiquantitatively using cytochemical method of Barka and Anderson. Peripheral blood lymphocytes in mice fed a low-Zn diet exhibited statistically significant lowering of the intracellular enzyme activity when compared with control groups. Absolute count of enzyme-positive lymphocytes was also significantly lowered. The Authors discuss the importance of their observations for evaluation of immune reactivity in trace-elements-deficient animals.

Acid Phosphatase↗
PubMed1985

Genetic polymorphism of erythrocyte acid phosphatase in Indian populations.

The polymorphism of erythrocyte acid phosphatase has been investigated in seven endogamous caste groups of Patiala and Faridkot districts of Punjab in north-west India. The frequency of the Pa allele in these groups varies from 26.8 to 38.3%, but there is no evidence for any significant heterogeneity in the total sample. The Pc allele is present in some of the groups, though in non-polymorphic proportions. Furthermore, the distribution of this polymorphism in Indian populations has been examined using gene frequency data available in the literature. The present study shows that while no clinal component is discernible in the distribution of this red cell enzyme in India, the populations of north India stand out with comparatively high Pa and Pc frequencies, and in almost all regions the incidence of these two alleles is higher in the non-tribals as compared to the tribals. The possible causes of this heterogeneity are discussed.

Acid Phosphatase↗
PubMed1991

Hydrolytic reactions in two-phase systems. Effect of water-immiscible organic solvents on stability and activity of acid phosphatase, beta-glucosidase, and beta-fructofuranosidase.

The stability and activity of three hydrolytic enzymes, acid phosphatase (EC 3.1.3.2), beta-fructofuranosidase (EC 3.2.1.26), and beta-glucosidase (EC 3.2.1.4), were studied at 30 degrees C in two-phase systems. They were prepared with equal quantities of buffered water and a water-immiscible organic solvent. Low-molecular-weight acetates and paraffins were tested in this investigation. The kinetic constant of storage inactivation was correlated with the logarithm of solvent polarity. Enzyme stability in the presence of organic phases, whose log P value was included in 1.2-2.2, was greater than the one measured in pure buffered aqueous media. On the other hand, a dramatic enzyme denaturation took place making use of solvents at higher log P-value. Experiments carried out during the 24-h operation clarified that the reaction yield does not depend solely on solvent polarity. Acid phosphatase and beta-glucosidase, which are less resistant than beta-fructofuranosidase to temperature and shear in buffered solutions, showed especially significant enhancement of catalytic activity when hydrolysis was performed with the addition of acetates (50% v/v).

Acetates↗
PubMed1982

Detection of a g' = 1.74 EPR signal in bovine spleen purple acid phosphatase.

When purified with hydroxylapatite, bovine spleen purple acid phosphatase, bearing two iron atoms/molecule, is EPR-silent. In contrast, enzyme purified without hydroxylapatite exhibits the distinctive g' = 1.74 EPR signal characteristic of porcine uteroferrin, with an intensity accounting for about 10% of the total iron. The intensity of the signal is increased 8-fold by the addition of ferrous iron. This treatment, while shifting the visible absorption maximum of the protein from 550 to 525 nm, does not significantly alter the intensity of its visible absorption. Loss of the g' = 1.74 EPR signal upon addition of phosphate to EPR-active preparations and the detection of virtually stoichiometric amounts of phosphate in the protein as isolated suggest that phosphate-binding may abolish the g' = 1.75 EPR signal. Such binding may bring the two iron atoms of the enzyme into juxtaposition, causing loss of EPR signal intensity either through spin-lattice relaxation broadening or antiferromagnetic exchange coupling, perhaps involving phosphate or other ligands intercalated between the two paramagnetic iron atoms.

Acid Phosphatase↗
PubMed1992

Pattern of leucocyte acid phosphatase reaction in T-cell lymphoblastic leukaemia.

Acid phosphatase (AP) reaction is a specific cytochemical marker for T-cell lymphoblastic leukaemia (T-ALL). Twenty six cases of ALL were diagnosed as T-ALL employing cytochemical profiles including AP and sheep red blood cell rosettes. Three district patterns of AP reaction were observed. On one end of the spectrum, 100% of the positive blasts showed the classical dot-like reaction while on the other 100% showed a scattered reaction. Between the two a mixed pattern was observed with 30-80% of the positive blasts showing the dot-like reaction while the rest showed scattered pattern. Dot-like pattern showed L1 morphology, high counts and low SRBC rosettes while scattered showed L2 morphology, low counts and high SRBC rosettes. The pattern observed in our series differs from the dot-like reaction observed in T-ALL in the western series. We recommend that this pattern must be borne in mind when employing AP reaction for T-ALL diagnosis (JPMA 42: 151, 1992).

Acid Phosphatase↗
PubMed1986

Prostate-specific acid phosphatase in carcinoid tumors.

Although prostate-specific acid phosphatase (PASP) has been recognized as a specific marker of tissue of prostatic origin, several investigators have pointed out that some of the carcinoid tumours and islet cell tumours of the pancreas reacted immunohistochemically to PSAP. We investigated 50 cases immunohistochemically comprising 44 carcinoids of the G-I tract, 3 of the bronchus, 1 each of the ovary, kidney and middle ear. PSAP positive cases were, 30 in G-I tract, one each in ovary and kidney. Eighty percent of tumours of hindgut origin were positive. Apart from the immunohistochemical study, the content of PSAP in preoperative serum and tumour tissue was estimated in a case with a rectal carcinoid. Extremely elevated PSAP was confirmed in both the serum and tumour tissue. Neuroendocrine tumours such as pheochromocytoma, medullary thyroid carcinoma, and islet cell carcinoma were investigated as controls. No cells immunoreactive to PSAP were observed in these control cases. Prostate specific antigen was definitely negative in carcinoids. We would emphasize that PSAP may be an excellent marker of carcinoids especially when derived from hindgut.

Acid Phosphatase↗
PubMed1985

Studies of the purine analog associated modulation of human erythrocyte acid phosphatase activity.

The activity of the human erythrocyte acid phosphatase is modulated by a series of structural analogs of purine. The unsubstituted purine base does not affect the enzyme activity. Addition of a substituent at the number six position usually generates an analog which activates the enzyme while similar substitutions at the two position usually generate an inhibitor. Pyrimidines are generally ineffective as modulators while several modifications of the imidazole ring of the purine analogs do not abolish the modulator activity of the purine analog. The level of response to all active analogs is isozyme specific. Differences in apparent relative affinities among the modulators are noted. The modulators with a positive effect on enzyme activity, are effective in the presence of methanol which is more effective than H2O as a phosphate acceptor. These analogs act by enhancing the rate of transfer of phosphate to H2O, while decreasing the rate of transfer to methanol. The results suggest that the purine analogs may act by altering the rate of hydrolysis of the phosphoenzyme intermediate by H2O or may change the rate-limiting step in the catalytic mechanism.

Acid Phosphatase↗
PubMed1980

Nuclear binding of androgens and acid phosphatase activity in prostatic tumors of Nb rats.

A transplantable prostatic adenocarcinoma derived from the dorsal lobe of the prostate gland of an Nb rat was analyzed for the concentration of nuclear androgen-binding sites and the presence of acid phosphatase activity. When extracts of nuclei from normal prostatic tissue were labelled with [1,2-3H]dihydrotestosterone in the absence and presence of competitor, two types of specific binding were observed: type 1 was characterized by an association constant (Ka) of 6 x 10(7) M-1 and involved a molecule that was excluded from Sephadex G-200; type 2 was characterized by a Ka of 3 x 10(8) M-1 and depended on a binding component that was retained by Sephadex G-200. Nuclei from androgen-stimulated tumors contained reduced concentrations of both androgen-binding components, whereas nuclei from autonomous tumors had only a trace amount of type 1 sites and were entirely devoid of type 2 sites. In all tumors the acid phosphatase activity per mg of protein was markedly elevated. Relative to normal, the activity of this enzyme was 140% and 350% higher in androgen-stimulated and autonomous tumors, respectively. These findings indicate that prostatic tumors are characterized by a decrease in nuclear androgen-binding, and an increase in specific activity of acid phosphatase, and also that such changes are more pronounced in autonomous than in androgen-stimulated tumors.

Acid Phosphatase↗
PubMed1998

Tyrosine phosphorylation of c-ErbB-2 is regulated by the cellular form of prostatic acid phosphatase in human prostate cancer cells.

Human prostatic acid phosphatase (PAcP) is a prostate epithelium-specific differentiation antigen. In prostate carcinomas, the cellular PAcP is decreased. We investigated its functional role in these cells. Several lines of evidence support the hypothesis that cellular PAcP functions as a neutral protein-tyrosine phosphatase and is involved in regulating prostate cell growth. In this study, we identify its in vivo substrate. Our results demonstrated that, in different human prostate cancer cell lines, the phosphotyrosine (Tyr(P)) level of a 185-kDa phosphoprotein (pp185) inversely correlates with the cellular activity of PAcP. On SDS-PAGE, this pp185 co-migrates with the c-ErbB-2 oncoprotein. Immunodepletion experiments revealed that c-ErbB-2 protein is the major pp185 in cells. Results from subclones of LNCaP cells indicated the lower the cellular PAcP activity, the higher the Tyr(P) levels of c-ErbB-2. This inverse correlation was further observed in PAcP cDNA-transfected cells. In clone 33 LNCaP cells, L-(+)-tartrate suppresses the cellular PAcP activity and causes an elevated Tyr(P) level of c-ErbB-2 protein. Epidermal growth factor stimulates the proliferation of LNCaP cells, which concurs with a decreased cellular PAcP activity as well as an increased Tyr(P) level of c-ErbB-2. Biochemically, PAcP dephosphorylates c-ErbB-2 at pH 7.0. The results thus suggest that cellular PAcP down-regulates prostate cell growth by dephosphorylating Tyr(P) on c-ErbB-2 oncoprotein in those cells.

Acid Phosphatase↗
PubMed1991

Human prostatic acid phosphatase directly stimulates collagen synthesis and alkaline phosphatase content of isolated bone cells.

Human prostatic acid phosphatase (hPAP) directly enhances the differentiated characteristics of isolated bone cells in vitro. This enzyme, when added to cell cultures for 24 h in vitro stimulates collagen synthesis and the production of alkaline phosphatase. The effects are dose dependent, with statistically significant effects occurring from 0.1-100 nM hPAP. Concentrations higher than 100 nM do not evoke greater effects. The maximal effect of hPAP occurs between 12 and 24 h of exposure. The cells stimulated to the greatest degree are osteoprogenitor cells and osteoblasts. Fibroblasts isolated from the same tissue show a lesser sensitivity to hPAP. hPAP has no detectable effect on cell proliferation, as measured by radiolabeled thymidine incorporation or total DNA synthesis. None of the observations reported in this work can be attributed to contaminating proteins in the hPAP preparation. hPAP was radiolabeled with 125I and was used for affinity binding and cross-linking studies. Scatchard analysis of specific binding indicated the presence of 1.0 X 10(5) high affinity binding sites/cell, with a Kd of 6.5 nM. Cross-linking studies demonstrated the presence of one 320-kDa binding complex. The pH profile and kinetic determinations of Km and maximum velocity for hPAP were similar to those previously reported, except for the finding of positive cooperativity of the substrate with the enzyme under the conditions of our assay. We believe that the direct stimulation of bone-forming cells by hPAP may contribute to the sclerotic nature of skeletal bone around sites of neoplastic prostatic metastases and that the effect of the enzyme is probably mediated by a plasma membrane receptor.

Acid Phosphatase↗
PubMed2001

A novel method for enzyme immobilization: direct encapsulation of acid phosphatase in nanoporous silica host materials.

Immobilization of acid phosphatase (ACP) in mesoporous or, more generally, nanoporous silica has been accomplished via the sol-gel reactions of tetramethyl orthosilicate in the presence of ACP and of D-glucose (DG) as a nonsurfactant template, which is subsequently removed by water extraction after the formation of nanocomposite gels. Characterization of the silica host after the removal of DG shows that the pore size and volume generally increase with the DG content. At high DG contents, the silica hosts are nanoporous with interconnected nanoscaled pores/channels of regular diameter (e.g., 3.4 nm). Catalytic activity of ACP encapsulated in nanoporous hosts is significantly improved over that in microporous host prepared in the absence of DG. The apparent enzymatic activity at various pH values and substrate concentrations correlates well with the nanostructures of the host matrices. As the DG content is increased in the synthesis, the activity tends to increase. At a DG content of 42-60 wt%, the samples exhibit activities about triple that of the template-free control. These and other results from enzymatic kinetic studies suggest that the increase in the pore size and volume facilitates the transport of the substrate and product molecules in the host matrices, leading to the observed increase in activity. The thermal stability of ACP is remarkably improved upon immobilization. There is no detectable leakage of ACP from the host matrices and the biogels are reuseable. This study provides a useful protocol for the development of nanotechnology for various biocatalysts and biosensors.

Acid Phosphatase↗
PubMed1986

Immunoultrastructural demonstration of prostatic acid phosphatase isoenzyme 2 in prostatic carcinoma.

Human prostatic acid phosphatase isoenzyme 2 (HPAcP-2) was isolated from semen. This purified enzyme was immunized to rabbit to produce polyclonal antibodies. The specificity of the antibodies was tested by Western blot transfer method. Rabbit IgG-peroxidase conjugate was prepared from the antiserum and used to localize HPAcP-2 in prostatic carcinoma. It was found that in the tumor glandular acinus the normal basal cells were replaced by tumor cells containing reaction product. In the tumor cells, the reaction product was seen in the cisternae of rough endoplasmic reticulum (ER) and Golgi apparatus. The secretory vesicles which contained reaction product-stained granules and some amorphous material were seen to fuse with the apical plasma membrane and discharged their content into the glandular lumen. On the other hand, some secretory vesicles in the tumor cells facing to the basement membrane also discharged their similar content into the extracellular spaces. Reaction product-stained granules were found in the interstitial spaces surrounding the tumor cells. These findings suggest that HPAcP-2 is synthesized on the bound ribosomes and discharged into the cisternae of rough ER. The molecules are transported to the Golgi cisternae. After concentration and packaging, HPAcP-2 molecules are then transferred to the secretory vesicles, and discharged into the glandular lumen and to the extracellular spaces. The isoenzyme released in the extracellular space may reach the blood stream through the interstitial spaces or the lymphatic system, resulting in the elevation of serum HPAcPase level in some prostatic cancer patients.

Acid Phosphatase↗
PubMed1971

Colorimetric determination of serum acid phosphatase activity using adenosine 3'-monophosphate as substrate.

The hydrolysis of adenosine 3'-monophosphate by serum acid phosphatase has been coupled to the liberation of ammonia from the adenosine generated through the action of exogenous adenosine deaminase. The ammonia is measured at the end of the incubation by a modification of the phenol-hypochlorite reaction of Berthelot. Optimum conditions for the enzyme reaction have been defined. Inhibition of the Berthelot reaction by the serum used in the assay is small, and may be compensated by a correction factor. Although the value for the control is high in relation to the test over the normal range, this is largely outweighed by the good sensitivity and precision of the method. The substrate is not significantly hydrolysed by erythrocyte acid phosphatase within the limits encountered in haemolysed sera. Experience of the method in routine hospital diagnosis compared favorably with that of a standard method employing disodium phenyl phosphate as substrate. It is suggested that activities greater than 3.1 IU/l should be further investigated and those greater than 3.7 IU/l should be regarded as definitely raised. The stability of human serum AcPase when promptly separated and held at 4 degrees C or - 20 degrees C was confirmed. At room temperature, acidification to pH 6.0 greatly improved stability.

Acid Phosphatase↗
PubMed1987

The response of poorly differentiated prostatic tumors to staining for prostate specific antigen and prostatic acid phosphatase: a comparative study.

A comparative study was done of the usefulness of immunohistochemical stains for prostate specific antigen and prostatic acid phosphatase in 20 poorly differentiated prostatic tumors. The stain for prostatic acid phosphatase was preferable to the prostate specific antigen stain not only because it was more intense and, therefore, more visible but also because it often was positive in areas in which an equivocal or negative stain was obtained with prostate specific antigen.

Acid Phosphatase↗
PubMed2003

Correlation of trace mineral concentrations with fructose, gamma-glutamyl transpeptidase, and acid phosphatase in seminal plasma of different categories of infertile men.

The study describes the concentrations of zinc, magnesium, copper, iron, and biochemical markers of seminal vesicle and prostate in seminal plasma of different categories of infertile men. The zinc level in oligasthenospermic subjects was significantly higher than in azoospermic, asthenospermic, and oligospermic subjects. The gamma-glutamyl transpeptidase activity in both oligoasthenospermic and azoospermic subjects were significantly lower than in asthenospermic and oligospermic individuals. There was no significant difference in iron, copper, and magnesium levels and acid phosphatase activity among the different infertile categories. A positive correlation between zinc and acid phosphatase (r=0.84, r= 0.73; p < 0.05), and between copper and fructose (r=0.81, r=0.72; p<0.05) was observed in oligoasthenospermic and azoospermic men, respectively. On the basis of our results, it may be postulated that there is a direct effect of the trace elements zinc and copper on acid phosphatase and fructose, respectively, in oligoasthenospermic and azoospermic subjects.

Acid Phosphatase↗
PubMed1987

Acid phosphatase activity in pre- and post-spawning hake (Merluccius hubbsi).

1. The specific activity of muscle acid phosphatase (E.C. 3.1.3.1.) in pre- and post-spawning hake was investigated. 2. Specific activity values, 0.54 in pre-spawning hakes and 1.64 in post-spawning fish, have been obtained. 3. Using a histochemical test, acid phosphatase has been localized mainly in the connective tissue. The strongest reaction has been observed in post-spawning hake. 4. The increase of the lysosomal activity in the connective tissue may be related to the changes found in the muscle texture associated with spawning.

Acid Phosphatase↗