scholarly journals Phosphatase activity of Poa pratensis seeds. III. Effect of fluoride, citrate, urea and other substances on the activity of acid phosphatase Ia2 and Ia3

2015 ◽  
Vol 47 (1–2) ◽  
pp. 83-89
Author(s):  
Irena Lorenc-Kubis ◽  
Bronisław Morawiecka
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Mixed Type ◽  
Poa Pratensis ◽  
Acid Phosphatases ◽  
Other Substances ◽  
Inhibited Acid ◽  
Hydrolysis Of

Effects of fluoride, citrate, urea and other substances on the activity of acid phosphatase a<sub>2</sub> and a<sub>3</sub> toward p-nitrophenylphosphate and phenylphosphate were investigated. Both enzymes were inhibited by fluoride, p-chloromercuribenzoate and oxalate. Fluoride inhibited acid phosphatase a<sub>2</sub> noncorapetitively with p-mitrophenylphosphate, whereas acid phosphatase a<sub>3</sub> showed inhibition of mixed type. Hydrolysis of phenylphosphate by both acid phosphatases was activated by citrate. Cytosine and uridine inhibited the activity of phosphatase a<sub>2</sub> toward p-nitrophenylphosphate and phenylphosphate, but no effect was observed in case of acid phosphatase a<sub>3</sub>. After 30 min. incubation with 4 M urea both enzymes lost about 30% of activity.

scholarly journals Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3

2015 ◽  
Vol 44 (2) ◽  
pp. 255-263 ◽  
Author(s):  
I. Lorenc-Kubis ◽  
B. Morawiecka ◽  
M. Niezgódka ◽  
A. Hebrowska
Keyword(s):  
Acid Phosphatase ◽  
Mixed Type ◽  
Poa Pratensis ◽  
Maximal Activity ◽  
Molecular Forms ◽  
Acid Phosphatases ◽  
Purification And Characterization ◽  
Inorganic Pyrophosphate ◽  
Nitrophenyl Phosphate

Two acid phosphatases (Ia2, Ia3) have been isolated from <i>Poa pratensis</i> seeds and partially purified. Both enzymes showed maximal activity at pH 4,9. They exhibited high activity towards p-nitrophenyl phosphate, inorganic pyrophosphate and phenyl phosphate, much less activity towards glucose-6 phosphate, and mononucleotides. Phosphatases a<sub>2</sub> and a<sub>3</sub> differed in their activity towards ADP. Orthophosphate, fluoride and Zn<sup>2+</sup> were effective inhibitors. EDTA, β-mercaptoethanol and Mg<sup>2+</sup> activated phophatase a<sub>2</sub> but had no effect on phosphatase a<sub>3</sub>. Zn<sup>2+</sup> inhibited the activity of phosphatase a<sub>2</sub> noncompetitively, whereas phosphatase a<sub>3</sub> showed inhibition of mixed type. Trypsin, chymotrypsin and pronase had no effect on the enzyme activities of both molecular forms.

Polyphosphate body and acid phosphatase localization in Nostoc sp.

1984 ◽  
Vol 30 (1) ◽  
pp. 8-15 ◽  
Author(s):  
John D. DuBois ◽  
Keith R. Roberts ◽  
Lawrence A. Kapustka
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Energy Stress ◽  
Nitrophenyl Phosphate ◽  
Carbon Compounds ◽  
Electron And Light Microscopy ◽  
Polyphosphate Bodies ◽  
Hydrolysis Of

Polyphosphate bodies and acid phosphatase activity were characterized in Nostoc sp. to determine if the hydrolysis of polyphosphate bodies occurs during dark (energy stress) periods. Electron and light microscopy were used to locate polyphosphate bodies. Acid phosphatase activity was measured using p-nitrophenyl phosphate as the substrate to determine net changes in the level of the enzyme activity. To induce energy stress, Nostoc sp. cells were kept in the dark for 72 h to deplete stored carbon compounds. Cells incubated in the light for 72 h (controls) showed acid phosphatase activity localized around the perimeter of polyphosphate bodies. When cells were incubated in the dark, acid phosphatase activity occurred throughout the polyphosphate body matrix. However, complete hydrolysis of the polyphosphate body did not occur and the rate of acid phosphatase activity was not affected.

THE DETERMINATION OF URINARY ACID PHOSPHATASES

1952 ◽  
Vol 30 (1) ◽  
pp. 1-9
Author(s):  
G. E. Delory ◽  
Merle Hetherington
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Convenient Method ◽  
Acid Phosphatase Activity ◽  
Acid Phosphatases ◽  
Urinary Acid

The effect of dilution on the apparent acid phosphatase activity of undialyzed and dialyzed urine has been studied. In the former case, the apparent activity increases with dilution but this anomaly is removed by a preliminary dialysis. A convenient method for the determination of acid phosphatase based on this observation is described.

GENETIC STUDIES OF ISOZYMES IN NEUROSPORA. I. A STUDY OF EIGHT SPECIES

1971 ◽  
Vol 13 (2) ◽  
pp. 298-305 ◽  
Author(s):  
M. Mohan Reddy ◽  
S. F. H. Threlkeld
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Starch Gel Electrophoresis ◽  
Acid Phosphatases ◽  
Genetic Studies ◽  
Starch Gel

Mycelial extracts of 34 strains representing eight species of the genus Neurospora were subjected to acrylamide and starch gel electrophoresis to detect sites of esterase, lactate dehydrogenase, amylase, peroxidase, and acid phosphatase activity. Nine isozymes of esterases, four isozymes of lactate dehyrogenases, three isozymes of peroxidases, and two isozymes of acid phosphatases were detected on the gels for the species. The application of zymograms as a biochemical means to characterize species is discussed.

scholarly journals OBSERVATIONS ON THE ACID PHOSPHATASES OF EUGLENA GRACILIS

1965 ◽  
Vol 24 (2) ◽  
pp. 223-234 ◽  
Author(s):  
Jacob J. Blum
Keyword(s):  
Cell Division ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Actinomycin D ◽  
De Novo ◽  
Fluoride Concentration ◽  
Acid Phosphatases ◽  
De Novo Synthesis ◽  
Increased Activity

When a bleached strain of Euglena is maintained in a medium containing very low con centrations of phosphate, the acid phosphatase activity increases. The increase in acid phosphatase activity is prevented by Actinomycin D and by p-fluorophenylalanine (PFA), indicating that the increased activity is due to de novo synthesis of acid phosphatase. When phosphate is replenished, the acid phosphatase activity decreases to the level characteristic of uninduced cells before there is any appreciable cell division. When cell division resumes in the presence of PFA, the level of acid phosphatase activity remains approximately constant. This indicates that there are two different phosphatases: a constitutive enzyme, whose synthesis is insensitive to the presence of PFA, and an induced enzyme, whose synthesis is sensitive to PFA. These enzymes are not equally sensitive to changes in pH and in fluoride concentration, thus permitting them to be assayed individually in whole toluene-treated cells. Induced cells also acquire the ability to remove phosphate from the medium very rapidly.

QUANTITATIVE STUDIES ON ISOLATED PANCREATIC ISLETS OF MAMMALS

1964 ◽  
Vol 45 (3) ◽  
pp. 476-486 ◽  
Author(s):  
Claes Hellerström ◽  
Inge-Bert Täljedal ◽  
Bo Hellman
Keyword(s):  
Acid Phosphatase ◽  
B Cells ◽  
Pancreatic Islets ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
List Type ◽  
Acid Phosphatases ◽  
Isolated Pancreatic Islets ◽  
Quantitative Studies ◽  
Tissue Homogenates

ABSTRACT Quantitative studies of non-specific acid phosphatases were performed on isolated pancreatic islets from obese-hyperglycaemic mice. The islets of these animals are composed of a rather pure population of B cells. The following observations were made: Acid phosphatases originating in the islet tissue, showed maximal enzyme activities at about pH 3.5 and 5.3 using p-nitrophenyl phosphate as substrate. The acid phosphatase activity of the exocrine tissue showed a single distinct maximum at about pH 5.3. The islet acid phosphatases were inhibited by sodium fluoride, sodium tartrate and formaldehyde. They were stable against storage in crude tissue homogenates at + 4° C and + 20° C for 48 hours. The pancreatic islets exhibited a significantly higher acid phosphatase activity than the exocrine parenchyma. Starvation for 7 days did not alter the enzyme levels in the islets or acini when measured at pH 5.3, while a probably increased enzyme activity was obtained in both these regions at pH 3.5. There was no evidence for a relationship between the insulin secretion and the acid phosphatase activity of the B cells.

scholarly journals Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad

2008 ◽  
Vol 38 (3) ◽  
pp. 650-657 ◽  
Author(s):  
Luciane Almeri Tabaldi ◽  
Raquel Ruppenthal ◽  
Luciane Belmonte Pereira ◽  
Denise Cargnelutti ◽  
Jamile Fabbrin Gonçalves ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphate Esters ◽  
Acid Phosphatases ◽  
Simple Preparation ◽  
Toxicological Studies ◽  
Plant Enzymes ◽  
Optimum Ph ◽  
Ph Range ◽  
Hydrolysis Of ◽  
Assay Conditions

Acid phosphatases (3.1.3.2) are a group of enzymes widely distributed in nature, which catalyze the hydrolysis of a variety of phosphate esters in the pH range of 4-6. We confirmed the presence of acid phosphatases in seedlings of cucumber (Cucumis sativus), radish (Raphanus sativus) and rocket salad (Eruca vesicaria) under different assay conditions using a rapid and simple preparation. The results showed that the optimum pH and temperature used for all species were close to 5.5 and 35°C, respectively. The enzyme was inhibited by molybdate, fluoride, azide, levamisole, orthovanadate, Zn2+ and Cu2+. Suramin had no effect on enzyme activity. The acid phosphatase from cucumber, radish and rocket salad hydrolyzed a wide variety of phosphate esters and the highest activity was observed with PPi, ATP and GTP. These results demonstrate that the enzyme investigated in this study is different from well known ester phosphate cleaving plant enzymes (apyrase and inorganic pyrophosphatases) and this preparation could be a useful tool to future toxicological studies and to study initially all isoforms of acid phosphatase.

THE EFFECT OF FORMALIN AND OF L-TARTARIC ACID ON SOME TISSUE ACID PHOSPHATASES

1961 ◽  
Vol 39 (4) ◽  
pp. 737-738 ◽  
Author(s):  
G. E. Delory ◽  
Merle Hetherington
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Tartaric Acid ◽  
Human Tissue ◽  
Acid Phosphatase Activity ◽  
Inhibitory Effect ◽  
Acid Phosphatases ◽  
Tissue Extracts

The inhibitory effect of 0.5% formalin and of 0.02 ML-tartaric acid has been studied on the acid phosphatase activity of a number of human tissue extracts. It was found that the sum of the formalin resistant and of the tartaric acid resistant enzyme activity closely approximated the activity of the uninhibited enzyme.

Some properties of a Ca2+- and (or) Mg2+-requiring nucleoside di- and tri-phosphatase(s) associated with the membranes of rat pancreatic zymogen granules

1978 ◽  
Vol 56 (6) ◽  
pp. 565-576 ◽  
Author(s):  
Francis Harper ◽  
François Lamy ◽  
Raymond Calvert
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Active Site ◽  
Acid Phosphatase Activity ◽  
Plasma Membranes ◽  
Zymogen Granules ◽  
Tentative Conclusion ◽  
Data Support ◽  
Single Protein ◽  
Hydrolysis Of

Membranes of rat pancreatic zymogen granules have been purified and found to be essentially free of contamination by mitochondria, microsomes, and plasma membranes. They possessed an acid phosphatase activity which derived probably from lysed lysosomes contaminating the purified zymogen granules from which the membranes were prepared. These membranes were found to contain a strong Ca2+- and (or) Mg2+-requiring activity toward all nucleoside di- and tri-phosphates. Various data support the tentative conclusion that a single protein catalyzes the hydrolysis of the nucleoside di- and tri-phosphates. This protein appears to be intrinsic with its active site localized on the internal face of the membranes.

Sign in / Sign up

Export Citation Format

Share Document