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At least 1,207 records · Page 67Linked to original sources
PubMed1989

Comparison of the property of a novel isozyme E (formerly null mutant, O) with other isozymes of hemolymph acid phosphatase of the silkworm.

1. A novel acid phosphatase isozyme E (formerly null mutant 0) was partially purified by ammonium sulfate fractionation, DEAE-Sephacel and Sephacryl S-200 column chromatography, and its properties were compared with those of other isozymes of the silkworm hemolymph. 2. The isozyme E was extremely heat labile and showed lower pH-stability than those of others. 3. Three isozymes hydrolyzed p-nitrophenyl phosphate, alpha-naphthyl phosphate, alpha-naphthyl phosphate and glucose-1-phosphate strongly. The isozyme E showed about 50% hydrolyzing activity for alpha-naphthyl phosphate as compared to those of A and B. 4. Activities of three isozymes were inhibited by tartaric acid, sodium fluoride, ammonium molybdate and potassium diphosphate. Inhibitory effects of Cu(2+) and HG(2+) were most remarkable against E isozyme.

Acid Phosphatase↗
PubMed1978

Human prostatic acid phosphatases: I. Isolation.

A new purification procedure is described for the human prostatic acid phosphatase. The procedure included carboxy-methyl-Sephadex and Concanavalin A affinity column chromatography. The purified enzyme has a high specific enzyme activity and is free from any extraneous proteins judging from immunochemical criteria and biochemical criteria such as SDS-polyacrylamide gel electrophoresis. The purified enyzme produced a monospecific anti-PAP antisera in animals and this anti-PAP antibody did not cross-react with other human acid phosphatases.

Acid Phosphatase↗
PubMed1977

Isatin enzyme interactions. V. Activation of rat liver acid phosphatase.

Influence of Isatin on rat tissue acid phosphatase has been studied. It has an organ-specific effect, the liver enzyme is activated, the brain enzyme is inhibited while those of kidney and intestine are not affected. Isatin activation of the liver enzyme is of mixed type and pH dependent. Rat liver enzyme appears to require intact amino and sulfhydryl groups for activity. Isatin seems to combine with the enzyme through the sulfhydryl group of the latter.

Acid Phosphatase↗
PubMed1996

Unfolding pathway in red kidney bean acid phosphatase is dependent on ligand binding.

Structural basis for ligand-induced protein stabilization was investigated in the case of an acid phosphatase (red kidney bean purple acid phosphatase (KBPAP)) from red kidney bean. Phosphate, a physiological ligand, increases the stability against solvent denaturation by 3.5 kcal/mol. Generality of phosphate stabilization was shown by similar effects with other KBPAP ligands viz. adenosine 5'-O-(thiotriphosphate), a nonhydrolyzable ligand, and arsenate, an inhibitor. The dissociation constant of phosphate obtained from denaturation curves matches with the dissociation constant estimated by conventional methods. The guanidinium chloride-mediated denaturation of KBPAP was monitored by several structural and functional parameters viz. activity, tryptophan fluorescence, 8-anilinonaphthalene 1-sulfonic acid binding, circular dichroism, and size exclusion chromatography, in the presence and absence of 10 mm phosphate. In the presence of phosphate, profiles of all the parameters shift to a higher guanidinium chloride concentration. Noncoincidence of these profiles in the absence of phosphate indicates multistate unfolding pathway for KBPAP; however, in the presence of phosphate, KBPAP unfolds with a single intermediate. Based on the crystal structure, we propose that the Arg258 may have an important role to play in stabilization mediated by phosphate.

Acid Phosphatase↗
PubMed1978

The light and electron microscopic distribution of acid phosphatase activity in human normal oesophageal epithelium.

Acid phosphatase activity in human normal oesophageal epithelium was studied with light and electron microscopic techniques. The maximum activity was found to be in the prickle and lower functional layers. Electron microscopic examination revealed activity to be localized in GERL, lysosomes and membrane coating granules. These last structures probably secreted their content into the intercellular space in the central part of the functional layer. Thick sections (0.5 micron) with tilting showed GERL to consist of anastomosing tubules.

Acid Phosphatase↗
PubMed1982

The acid phosphatase with optimum pH of 2.5 of Escherichia coli. Physiological and Biochemical study.

In Escherichia coli, the physiological conditions governing the expression of an acid phosphatase with an optimum pH of 2.5 were determined. By contrast with most enzymes, the synthesis of this phosphatase was turned off in exponentially growing bacteria and started as soon as cultures entered the stationary phase. A starvation for inorganic phosphate resulted in a premature full induction, while carbon, nitrogen, and sulfur limitations were inefficient. In the presence of nonlimiting amounts of inorganic phosphate, however, the transfer of the culture to anaerobic conditions led to an immediate accumulation of the acid phosphatase. Cyclic AMP exerted a strong negative control on the biosynthesis and of this enzyme for which the integrity of both the cya and the crp gene functions was necessary. The acid phosphatase was purified to apparent homogeneity and behaved as a monomeric protein with a molecular weight of about 45,000. It had predominantly a phosphoanhydride phosphatase activity and preferentially hydrolyzed the gamma-phosphoryl residue of GTP (Km = 0.35 mM) and the 5'-beta-phosphoryl residue of ppGpp (Km = 1.8 mM). The corresponding beta-phosphoryl residue of GDP was little hydrolyzed, while CTP, ATP, and UTP were not. The enzyme did not split most phosphomonoesters with the exception of the synthetic substrate p-nitrophenyl phosphate (Km = 2.7 mM), 2,3-bisphosphoglycerate (Km = 5 mM), and fructose 1,6-bisphosphate (Km = 5 mM). It was competitively inhibited by tartaric acid and by sodium fluoride (Ki = 60 microM). In addition, it was sensitive to the inhibitor of the translation elongation factor EF-G fusidic acid, and was also strongly inhibited by the triazine dye Cibacron Blue F3GA (Ki = 0.3 microM), suggesting the existence of a site able to recognize nucleotides.

Acid Phosphatase↗
PubMedDate not supplied

[Characterization of Escherichia hermannii by electrophoresis of esterases, acid phosphatase and glutamate and malate dehydrogenases].

Esterases, acid phosphatase and glutamate and malate dehydrogenases of 11 strains of Escherichia hermannii were analysed by horizontal electrophoresis in polyacrylamide agarose gel. Seven esterase bands were defined by their range of activity on synthetic substrates and their sensitivity or resistance to di-isopropyl fluorophosphate. These bands were different in activity and in mobility from those produced by E. coli strains. On the basis of variations in mobility of glutamate and malate dehydrogenases and in the number and mobility of esterases, the strains were divided into 3 zymotypes.

Acid Phosphatase↗
PubMedDate not supplied

The use of acid phosphatase test papers for DNA profiling.

The acid phosphatase (AP) test is a routine assay used to screen casework items for the possible presence of semen. This colour test is carried out on filter paper which is retained after testing. Two-year-old AP test papers were found to contain sufficient DNA for short tandem repeat (STR) profiling. Prior to polymerase chain reaction (PCR) amplification, the DNA was preferentially separated into sperm depleted and sperm enriched cell fractions. The implication of these findings for past and present cases is discussed.

Acid Phosphatase↗
PubMed1984

Increased prostate-type acid phosphatase activity in serum and typical bone lesions simulating the presence of prostatic carcinoma.

In a man with myelomonocytic leukemia, the association of increased prostatic acid phosphatase activity in serum and the presence of typical bone lesions on roentgenography suggested the existence of disseminated prostatic carcinoma. During the clinical observation period, however, prostatic involvement could not be proved. Moreover, bone pain and prostatic-type acid phosphatase activity in serum closely paralleled monocyte counts and the degree of hepatosplenomegaly and leukemic skin lesions. Finally, meticulous postmortem examination of the prostate showed no prostatic carcinoma. This clinical picture appears to be entirely explicable in terms of leukemic organ infiltration and the proliferation of monocytes, which are known to contain acid phosphatase isoenzymes like those in the prostate.

Acid Phosphatase↗
PubMed2000

Substrate selectivity in Aspergillus niger KU-8 acid phosphatase II using phosphoryl oligosaccharides.

The intracellular acid phosphatase II (ACPase II) produced by Aspergillus niger KU-8 preferentially dephosphorylates C-6 phosphate groups rather than C-3 phosphate groups of phosphoryl oligosaccharides. In this study, the kinetic parameters of ACPase II were measured. 3(2)-phosphoryl maltotriose and 6(2)-phosphoryl maltotriose, which differ only in the binding position of the phosphate group, were prepared and used as the substrates. The Km for both substrates were similar. However, the k(cat) value for the 6(2)-phosphoryl maltotriose was about three-fold of that for the 3(2)-phosphoryl maltotriose.

Acid Phosphatase↗
PubMed1984

Erythrocyte acid phosphatase in human hair root sheaths.

Erythrocyte acid phosphatase (EAP) was observed in human hair root sheaths where hair sheaths and blood samples were collected from 150 donors. In each case, the hairs were typed first for EAP and then confirmed by typing the blood from the same donors. Of the 150 donors checked, EAP activity was found in 135 of the samples; the other 15 samples showed no activity because they contained no sheath cells. Of the 135 samples showing activity, 108 of those were typed accurately in EAP. The remaining 27 samples had EAP activity but with inconclusive findings. In this study, all six common phenotypes were encountered.

Acid Phosphatase↗
PubMed1983

Effects of work environment contaminated with benzene, toluene and xylene on acid phosphatase activity in lymphocytes.

The activity of acid phosphatase (AP) in peripheral blood lymphocytes was determined by means of histochemical method in 108 workers having occupational contact with organic solvents containing benzene and its homologues. Benzene, toluene and xylene concentrations in the air at work stands were equal to 0-370, 0-580 and 0-560 mg/eu.m., respectively. A progressing reduction of numbers of lymphocytes having AP-positive intact lysosomes was stated in workers with a working time equal 31-122 months. This phenomenon was more expressed in workers exposed to greater concentrations of benzene and its homologues. The damage to the lysosomal apparatus of lymphocytes reflected by an increased permeability of lysosomal membranes can be regarded as one of the earliest symptoms of toxic effects of benzene, toluene and xylene on cells of the lymphocytic series.

Acid Phosphatase↗
PubMed1977

Separation of tissue and serum acid phosphatase isoenzymes by ion-exchange column chromatography.

I describe a simple, rapid ion-exchange column-chromatographic technique for separating the acid phosphatase (EC 3.1.3.2) isoenzymes in human serum and tissue. Extracts of platelets, spleen, liver, erythrocytes, and prostate were used to determine optimum conditions for separating these isoenzymes. Samples layered on mini-colunms of DEAE-Sephadex A-50 were eluted stepwise with sodium chloride (100, 200, and 300 mmol/liter, buffered with tris (hydroxymethyl)aminomethane). Activity in column effluents was measured with p-nitrophenol phosphate as substrate, and their isoenzyme content was assessed by electrophoresis on polyacrylamide gel. Comparision of activity patterns so derived for various tissues revealed prostatic tissue to be a rich source of acid phosphatase isoenzyme 2 activity. Evaluation of sera from six patients with prostatic cancer revealed isoenzyme patterns with prominent amount of isoenzyme 2 (3.8 to 27.6 U/liter). sera from 10 healthy laboratory technicians contained isoenzyme 2 in the range of 0.3-0.5 U/liter. Samples from two patients with abnormally high activity owing to nonprostatic conditions (Gaucher's disease and carcinoma of lung) exhibited less than 2 U of isoenzyme 2 per liter and acid phosphatase isoenzymes 3-5 that were 50- to 100-fold the normal range. Quantification of isoenzyme 2 by DEAE-Sephadex column chromatography as described appears to provide a more sensitive and specific approach to diagnosis of prostatic cancer.

Acid Phosphatase↗
PubMed2000

Partial purification and characterization of thermostable acid phosphatase from thermoacidophilic archaeon Sulfolobus acidocaldarius.

Thermostable acid phosphatase (APase) from thermoacidophilic archaeon Sulfolobus acidocaldarius was isolated, partially purified, and characterized. The optimum pH and temperature of the enzyme for p-nitrophenylphosphate (pNPP) as a substrate were 5.0 and 70 degrees C, respectively. The apparent K(m) value was 1.9 mM. This APase showed a native molecular mass of 20 kDa on a gel filtration chromatography. Of the APase activity, 60% remained after 60 min of heat treatment at 75 degrees C. To confirm whether the APase is active in the monomeric form, we attempted to elute the enzyme from SDS-polyacrylamide gels with Disk electrophoresis apparatus and renature the enzyme. The APase activity was recovered up to 50% in the 14- to 35-kDa range, and maximum around 25 kDa. These results suggest that this APase is monomeric protein.

Acid Phosphatase↗
PubMed1986

Characterization of lysosomal acid phosphatase from normal and malignant mammary tissue.

Acid phosphatase (EC 3.1.3.2) isoenzyme 3 was purified from normal and malignant human mammary tissue and its properties in each were compared. The relative molecular mass of each was 53 000, as measured by sodium dodecyl sulfate gel electrophoresis. Several phosphomonoesters are good substrates for the isoenzymes, whereas organic and inorganic pyrophosphates and phosphoryl choline are hydrolyzed very slowly or not detectably. The optimum pH for interaction of these isoenzymes with p-nitrophenyl phosphate as substrate ranges from 3.5 to 4.5. L-(+)-Tartrate is a very strong inhibitor, Ki = 0.028 +/- 0.04 mmol/L (mean +/- SE), as are mercuric and fluoride ions in low concentrations. We conclude that type 3 isoenzymes obtained from normal and malignant tissue are very similar, though the malignant tissue appears to have a greater proportion of this type than does normal tissue.

Acid Phosphatase↗
PubMed1988

Characterization of Yersinia enterocolitica, Y. intermedia, Y. aldovae, Y. frederiksenii, Y. kristensenii and Y. pseudotuberculosis by electrophoretic polymorphism of acid phosphatase, esterases, and glutamate and malate dehydrogenases.

Acid phosphatase, esterases, and glutamate and malate dehydrogenases of 192 strains of Yersinia enterocolitica, Y. intermedia, Y. aldovae, Y. frederiksenii, Y. kristensenii and Y. pseudotuberculosis were analysed by horizontal polyacrylamide agarose gel electrophoresis and by isoelectrofocusing in thin-layer polyacrylamide gels. The six species were clearly separated from each other by their distinct enzyme electrophoretic polymorphism. For Y. enterocolitica, the strains of biotype 5 were differentiated from the other biotypes by the mobility of glutamate dehydrogenase. For Y. frederiksenii, six zymotypes were delineated by pI and by the mobility of the enzymes. Variation in number or mobility of esterases within each species could represent a marker for epidemiological and ecological analyses. A linear relationship was obtained between the mean genetic diversity coefficient of enzymes and the mean percentage DNA-DNA relatedness of Y. intermedia, Y. aldovae, Y. enterocolitica and Y. frederiksenii.

Acid Phosphatase↗
PubMed2006

[Prognosis of prostate cancer with elevated prostatic acid phosphatase].

To evaluate the significance of prostatic acid phosphatase (PAP), we analyzed 1,029 prostate cancer patients who were treated at the Niigata Cancer Center. We classified clinically localized prostate cancer with elevated PAP as stage DO. When stage DO was not taken into acount, the 5-year cause-specific survival rate for stage A, B, C and D was 94.7, 97.9, 87.7 and 42.4%, respectively. Taking stage DO into account, the cause-specific survival curve for stage DO patients was similar to those for stage B,C patients. The 5-year cause-specific survival rate for stage DO was 92.2% considering above 3 ng/ml as elevated PAP. A significant correlation was found between PAP and cause-specific survival for all cases but no correlation was found for non-metastatic disease patients. The significance of PAP in the staging of prostate cancer is limited.

Acid Phosphatase↗