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PubMed1977

Localization of acid phosphatase in Saccharomyces cerevisiae: a clue to cell wall formation.

Acid phosphatase is present in two layers of the cell envelope of Saccharomyces cerevisiae. These are separated by another layer, which is free of acid phosphatase. We have evidence that the cell wall is built up in two stages, which are independent. In the first stage, the cell wall is built up during the formation of the bud. Glucanase vesicles are involved in this process. In the second stage, a thick layer is deposited at the inside against the new cell wall. This results in the thick, rigid wall of the mature yeast cell. This latter layer is probably assembled on the outer surface of the plasmalemma.

Acid Phosphatase↗
PubMed1982

Acid phosphatase and protease activities in immobilized rat skeletal muscles.

The effect of hind-limb immobilization on selected lysosomal enzyme activities was studied in rat hind-limb muscles composed primarily of type I, IIA, or IIB fibers. Following immobilization, acid protease and acid phosphatase both exhibited significant (P less than 0.05) increases in their activity per unit weight in all three fiber types. Acid phosphatase activity increased at day 14 of immobilization in the three muscles and returned to control levels by day 21. Acid protease activity also changed biphasically, displaying a higher and earlier rise than acid phosphatase. The pattern of change in acid protease, but not acid phosphatase, closely parallels observed muscle wasting. The present data therefore demonstrate enhanced proteolytic capacity of all three fiber types early during muscular atrophy. In addition, the data suggest a dependence of basal hydrolytic and proteolytic activities and their adaptive response to immobilization on muscle fiber composition.

Acid Phosphatase↗
PubMed1988

Starfish acrosomal acid phosphatase: a cytochemical and biochemical study.

The acrosome reaction of spermatozoa from the starfish Marthasterias glacialis was induced with the ionophore A23187. Reacted cells were then processed for acid phosphatase ultrastructural cytochemistry, but significant enzyme activity was not detected. However, when the supernates from suspensions of ionophore-treated sperm were assayed for acid phosphatase, a net enzyme activity was observed. Supernatant proteins were run in starch gel electrophoresis and fluorescent zymograms revealed a single band of acid phosphatase. SDS-PAGE of proteins eluted from the active spots of starch gels showed one major band of about 63 kDa. The results obtained support the hypothesis that the acid phosphatase whose activity has been detected only at the time of binding of sperm and egg originates from the sperm acrosome.

Acid Phosphatase↗
PubMed1991

The essential tyrosine of the internalization signal in lysosomal acid phosphatase is part of a beta turn.

For rapid endocytosis lysosomal acid phosphatase requires a Tyr-containing signal in its cytoplasmic domain, as do cell surface receptors mediating endocytosis and clustering in coated pits. To determine the structure of the internalization signal an 18 amino acid peptide representing the cytoplasmic tail of lysosomal acid phosphatase was analyzed by two-dimensional nuclear magnetic resonance spectroscopy. Part of the peptide, 5-PPGY-8, forms a well-ordered beta turn of type I in solution. Our result and data on the structure of the endocytosis signal of the low density lipoprotein receptor reported by Bansal and Gierasch in the accompanying paper represent experimental determinations of the three-dimensional structure of protein transport signals and suggest that the essential aromatic amino acid of internalization signals is recognized by a putative cytoplasmic receptor in the structural context of a tight turn.

Acid Phosphatase↗
PubMed1965

Heat stabilities of acid phosphatases from pinto bean leaves.

Two acid phosphatases were demonstrable by polyacrylamide gel electrophoresis. They had different mobilities and different heat stabilities in 1.0M acetate buffer, pH 5.2. Both phosphatases had the same electro-phoretic mobility in tris buffer at pH 7.5, gave one boundary in the analytical ultracentrifuge in tris or acetate buffer, and had the same sedimentation coefficient. The difference in these properties suggests an alteration in conformation of the proteins by the buffer systems.

Acid Phosphatase↗
PubMed1997

Overexpression of the Aspergillus niger pH 2.5 acid phosphatase gene in a heterologous host Trichoderma reesei.

An Aspergillus gene coding for a pH 2.5 acid phosphatase enzyme was successfully overexpressed in Trichoderma reesei under the strong main cellobiohydrolase I (cbh 1) promoter. The best transformants produced up to 240 times more of the acid phosphatase than the Aspergillus strain from which the phosphatase gene was originally isolated. The recombinant enzyme was effectively secreted into the culture medium both by its own and the cbh 1 secretion signal. The heterologous pH 2.5 acid phosphatase enzyme produced by the Trichoderma transformants was seen as four protein bands of about 55-66 kD resulting from variable glycosylation in Trichoderma. The activity of the recombinant enzyme was not affected. Enzyme preparations rich in both cellulose and phytate hydrolysing enzymes are of interest in the animal feed industry.

Acid Phosphatase↗
PubMed1989

Effect of Bacillus sphaericus and Bacillus thuringiensis on acid-phosphatase activity of mosquito larvae, Culex pipiens and Aedes caspius.

The use of Bacillus sphaericus and B. thuringiensis H-14 form one of the important group of biological control agent against mosquito larvae. Acid phosphatase enzyme plays a significant role in determining susceptibility of mosquito larvae to both bacterial species. Biochemical assay showed activation in acid phosphatase in Culex pipiens and Aedes caspius treated with B. thuringiensis. Variation in acid phosphatase activity occurred in both mosquitoes treated with B. sphaericus, while there was no change in acid phosphatase activity in A. caspius. An obvious increase in activity in C. pipiens treated with the same bacteria was observed.

Acid Phosphatase↗
PubMed1983

Studies on the structural basis of the heterogeneity of human prostatic and seminal acid phosphatases.

We studied possible causes of the electrophoretic heterogeneity of the acid phosphatase (EC 3.1.3.2) purified by affinity chromatography from human prostate and human seminal fluid. The isoelectric focusing pattern in polyacrylamide gel shows numerous bands in the pH range 4.0-5.2 and 5.5-5.9. Treatment with neuraminidase under conditions shown to cause complete removal of sialic acid does not abolish the observed heterogeneity. Although there is a change of the more acidic forms to ones having more basic pI values, at least 4 distinct bands remain. Structural differences at the amino terminal end can be ruled out as the cause of the remaining electrophoretic heterogeneity. Lysine is shown to be the amino terminal amino acid for both the prostatic and seminal fluid enzymes. The sequences of the first 23 amino acids are shown to be identical for the prostatic and seminal fluid acid phosphatases. The functional enzyme contains no metal ion but it can be stoichiometrically inactivated by cupric ion.

Acid Phosphatase↗
PubMed1989

Rat adipose tissue phosphatidic acid phosphatase: lack of effect of nucleotides on cytosolic enzyme activity.

The soluble phosphatidic acid phosphatase from rat adipose tissue was partially purified using ammonium sulfate fractionation and hydroxyapatite chromatography. Administration of ethanol has been found to increase phosphatidic acid phosphatase activity. The enzyme activity has been found to be dependent on magnesium ions with maximal activity at 2-5 mM magnesium. The enzyme displays an apparent pH optimum of 7.0. The activity of the enzyme is not affected by addition of ATP or ADP, in contrast with the results for hepatic phosphatidic acid phosphatase. The results suggest that these two enzymes may be regulated by different mechanisms and that they may thus represent two different types of isoenzyme.

Adenosine Diphosphate↗
PubMed1992

Characterization of cationic acid phosphatase isozyme from rat liver mitochondria.

Acid phosphatase isozyme was highly purified from rat liver mitochondrial fraction. The enzyme showed an isoelectric point value of above 9.5 on isoelectric focusing, and the apparent molecular weight was estimated to be 32000 by Sephadex G-100 gel filtration or 16000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme catalyzed the hydrolysis of adenosine 5'-triphosphate, adenosine 5'-diphosphate, thiamine pyrophosphate, inorganic pyrophosphate, and phosphoprotein such as casein and phosvitin, but not of several phosphomonoesters, except for p-nitrophenyl phosphate and o-phosphotyrosine. The enzyme was not inhibited by L-(+)-tartrate, and was significantly activated by Fe2+ and reducing agents such as ascorbic acid, L-cysteine,and dithiothreitol. The enzyme was found to be distributed in various rat tissues including liver, spleen, kidney, small intestine, lung, stomach, brain and heart, but not in skeletal muscle.

Acid Phosphatase↗
PubMed1976

Human red cell acid phosphatase: quantitative evidence of a silent gene PO, and a Danish population study.

In a forensic case of disputed paternity an apparent mother/child incompatibility with respect to red cell acid phosphatase was found, the mother appearing as type A and the child as type B. Determination of electrophoretic type and of acid phosphatase activity in 8 of the family members strongly suggested the presence of a silent gene PO in 4 of the individuals. The phosphatase levels in the four heterozygotes were about half the values expected from normal values determined in 100 healthy adults representing the different phenotypes. The distribution of red cell acid phosphatase types in 3,735 unrelated Danish adults and in 1,109 mother/child pairs is reported; gene frequencies Pa = 0.369, Pb = 0.566 and Pc = 0.065. The PO gene frequency was roughly estimated as 0.001. Results are reported on the application of the red cell acid phosphatase system to 300 2-men cases of disputed paternity.

Acid Phosphatase↗
PubMedDate not supplied

Immunochemical studies of prostatic acid phosphatase.

Immunologic specificity of the prostatic acid phosphatase (PAP) and the kinetics of the PAP-anti-PAP antibody interactions were studied in detail. Antigenic identity of electrophoretic isozymes of PAP was established in this study. Counterimmunoelectrophoretic assay, radioimmunoassay, and immunofluorescence technique were developed to detect PAP and PAP-synthesizing cells. These techniques were applied to the determination of serum PAP levels and to the identification of metastatic prostate cancer cells in biopsies.

Acid Phosphatase↗
PubMed1992

Protein-specific features of the general secretion pathway in yeast: the secretion of acid phosphatase.

The major phosphate-repressible acid phosphatase (APase) of Saccharomyces cerevisiae, a cell wall glycoprotein, has been extensively used as a reporter protein to analyse successive steps in the yeast secretory pathway. In contrast to other yeast secretory proteins, APase can still be translocated into the endoplasmic reticulum (ER) even when it is made without its signal peptide. This property illustrates the permissiveness of targeting to the ER in yeast. Studies on APase-containing hybrid proteins have provided some of the evidence that specific soluble factors must interact with secretory proteins prior to their translocation across the ER membrane. A systematic analysis of mutations affecting the sequence of the APase signal peptide cleavage site demonstrated that cleavage occurs only when the last amino acid of the signal sequence is small and neutral. This was one of the first studies to verify the requirements for signal peptidase cleavage that had previously only been predicted from statistical analysis. Studies performed either with inhibitors of glycosylation or with mutant APases demonstrated the critical role of core glycosylation for APase folding, which is essential for efficient transport beyond the ER. Following the fate of particular modified APases along the secretory pathway provided insights into some general properties of the secretory apparatus and illustrated the specific requirements for a given protein during its intracellular traffic.

Acid Phosphatase↗
PubMed1997

Continuous assay for acid phosphatase using 1-naphthyl phosphate as a substrate.

The described continuous acid phosphatase assay is based on kinetics of the release of 1-naphthol in the course of the enzyme-catalyzed hydrolysis of 1-naphthyl phosphate, measured at 320 nm in aqueous solution and at 322 nm in sodium-bis(2-ethylhexyl)sulfosuccinate isooctane-water reverse micelles in a broad pH range (1.0-8.2). The method allows precise determination of the initial rate of the reaction and therefore may be used in the steady-state and pre-steady-state studies on the phosphatase-catalyzed reaction. The kinetic parameters (Km and kcat) for human prostatic acid phosphatase in aqueous solution and in reverse micelles, at pH 3.8, 4.5 and 5.7, by the proposed 1-naphthyl phosphate assay have been determined.

Acid Phosphatase↗
PubMed1983

[Leukocyte acid phosphatase activity in myocardial infarct].

Leucocytic acid phosphatase (AP) activity was measured cytochemically in 21 myocardial-infarction patients aged 37 to 57. Neutrophil leucocytosis was found to result from an increase in the quantity of cells with high activity of the enzyme. Neutrophil AP activity was elevated during the first days of the infarction and dropped to the baseline level on day 14. Between days 7 and 14, the numbers of lymphocytes with cytoplasmatic AP localization were reduced, suggesting lysosome stabilization at this stage of myocardial infarction.

Acid Phosphatase↗
PubMedDate not supplied

Seminal fructose, citric acid and acid phosphatase before and after vasectomy in man.

Seminal fructose, citric acid and acid phosphatase were estimated from 23 healthy males before vasectomy and three months later. Each subject had children and the men volunteered for sterilization because other possibilities of contraception were inapplicable. Vasectomy was performed under local anesthesia in the conventional manner. Semen of all patients was azoospermic three months after vasectomy. In this study, the amounts of seminal fructose and citric acid were significantly higher after vasectomy than before operation. The activity of seminal acid phosphatase was a little less, but the difference was not significant. The increase of seminal fructose and citric acid could be explained by the lack of spermatozoa, which normally use them into their metabolism.

Acid Phosphatase↗
PubMed1987

Role of glycosylation in secretion of yeast acid phosphatase.

The minimal glycosylation requirement for acid phosphatase secretion and activity was investigated using tunicamycin, an inhibitor of protein glycosylation, and a yeast mutant defective in the synthesis of oligosaccharide outer chains. The results obtained show that outer chain addition is not essential for secretion of active enzyme and that only 4 core chains, out of 8 normally attached to a protein subunit, are sufficient for enzyme transport to the periplasmic space. Enzyme forms with less than 4 chains were retained in membranes of endoplasmic reticulum. Secreted underglycosylated enzyme forms are partially or completely inactive.

Acid Phosphatase↗
PubMed1988

Day-night variability in acid phosphatase activity of pineal gland macrophages.

Acid phosphatase (ACP) activity was investigated in the photoreceptive pineal gland of the goldfish by both light and electron microscopy. Intraluminal macrophages exhibited the greatest ACP reactivity that was generally confined to lysosomal bodies containing membranous debris. Quantitative light microscopic evaluation revealed significantly higher ACP reactivity in animals collected at mid-light compared to those collected at mid-dark suggesting that functional activities of macrophages in this photoneuroendocrine organ are cyclical over the 24-h photoperiod. Day-night differences in macrophage ACP activity may reflect rhythmic renewal and shedding of photoreceptor outer segment membranes.

Acid Phosphatase↗