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.

Acid phosphatase in Gaucher's disease.

1980 ◽  
Vol 26 (3) ◽  
pp. 371-382
Author(s):  
D B Robinson ◽  
R H Glew
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Purification And Characterization ◽  
Gaucher's Disease ◽  
Gaucher’S Disease ◽  
Intracellular Location ◽  
Increased Activity ◽  
Serum Acid Phosphatase

Abstract Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.

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.

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.

Acid phosphatase in Gaucher's disease.

1980 ◽  
Vol 26 (3) ◽  
pp. 371-382 ◽  
Author(s):  
D B Robinson ◽  
R H Glew
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Purification And Characterization ◽  
Gaucher's Disease ◽  
Gaucher’S Disease ◽  
Intracellular Location ◽  
Increased Activity ◽  
Serum Acid Phosphatase

Abstract Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.

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.

Recessive Mutations in ACP4 Cause Amelogenesis Imperfecta

2021 ◽  
pp. 002203452110151
Author(s):  
Y.J. Kim ◽  
Y. Lee ◽  
Y. Kasimoglu ◽  
F. Seymen ◽  
J.P. Simmer ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
De Novo ◽  
Tooth Enamel ◽  
Activity Level ◽  
Amelogenesis Imperfecta ◽  
Catalytic Core ◽  
Enamel Thickness ◽  
Mutant Forms

Amelogenesis imperfecta (AI) is an innate disorder that affects the formation and mineralization of the tooth enamel. When diagnosed with AI, one’s teeth can be hypoplastic (thin enamel), hypomature (normal enamel thickness but discolored and softer than normal enamel), hypocalcified (normal enamel thickness but extremely weak), or mixed conditions of the above. Numerous studies have revealed the genes that are involved in causing AI. Recently, ACP4 (acid phosphatase 4) was newly found as a gene causing hypoplastic AI, and it was suggested that mutant forms of ACP4 might affect access to the catalytic core or the ability to form a homodimer. In this study, a Korean and a Turkish family with hypoplastic AI were recruited, and their exome sequences were analyzed. Biallelic mutations were revealed in ACP4: paternal (NM_033068: c.419C>T, p.(Pro140Leu)) and maternal (c.262C>A, p.(Arg88Ser)) mutations in family 1 and a paternal (c.713C>T, p.(Ser238Leu)) mutation and de novo (c.350A>G, p.(Gln117Arg)) mutation in the maternal allele in family 2. Mutations were analyzed by cloning, mutagenesis, immunofluorescence, immunoprecipitation, and acid phosphatase activity test. Comparison between the wild-type and mutant ACP4s showed a decreased amount of protein expression from the mutant forms, a decreased ability to form a homodimer, and a decreased acid phosphatase activity level. We believe that these findings will not only expand the mutational spectrum of ACP4 but also increase our understanding of the mechanism of ACP4 function during normal and pathologic amelogenesis.

scholarly journals The development of ribonuclease and acid phosphatase during germination of Pisum arvense

1974 ◽  
Vol 142 (2) ◽  
pp. 211-219 ◽  
Author(s):  
Geoffrey R. Barker ◽  
Clifford M. Bray ◽  
Trevor J. Walter
Keyword(s):  
Amino Acids ◽  
Acid Phosphatase ◽  
Phase I ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
De Novo ◽  
Deuterium Oxide ◽  
Buoyant Density ◽  
Ribonuclease Activity ◽  
Supernatant Fraction

1. Development of ribonuclease activity in the cotyledons of germinating peas is biphasic, the time of appearance of the two phases depending on the conditions of growth. 2. Acid phosphatase exhibits a single phase of development. 3. Cycloheximide inhibits development of ribonuclease activity in phase II but not in phase I. 4.14C-labelled amino acids are not incorporated into ribonuclease isolated during phase I. 5. The buoyant density of ribonuclease isolated during phase I is not affected by imbibition of the seed in 80% deuterium oxide. 6. Acid phosphatase was isolated from the supernatant fraction of the cotyledons of germinating peas and partially purified. 7. Development of acid phosphatase activity during germination is inhibited by treatment of the seed with cycloheximide or actinomycin D. 8. Partial purification of acid phosphatase from peas germinated in the presence of14C-labelled amino acids suggests that the enzyme is radioactively labelled. 9. Germination of peas in the presence of 80% deuterium oxide results in an increase in the buoyant density of acid phosphatase. 10. The results suggest that increase in ribonuclease activity during the first 4 days of germination does not result from synthesis of protein de novo, but that the corresponding increase in acid phosphatase activity does result from synthesis de novo.

scholarly journals Moraxella catarrhalis Synthesizes an Autotransporter That Is an Acid Phosphatase

2007 ◽  
Vol 190 (4) ◽  
pp. 1459-1472 ◽  
Author(s):  
Todd C. Hoopman ◽  
Wei Wang ◽  
Chad A. Brautigam ◽  
Jennifer L. Sedillo ◽  
Thomas J. Reilly ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Moraxella Catarrhalis ◽  
Acid Phosphatase Activity ◽  
Cloning And Expression ◽  
Nucleotide Sequence Analysis ◽  
Acid Phosphatases ◽  
Terminal Portion ◽  
Phosphatase Domain ◽  
Translocation Domain

ABSTRACT Moraxella catarrhalis O35E was shown to synthesize a 105-kDa protein that has similarity to both acid phosphatases and autotransporters. The N-terminal portion of the M. catarrhalis acid phosphatase A (MapA) was most similar (the BLAST probability score was 10−10) to bacterial class A nonspecific acid phosphatases. The central region of the MapA protein had similarity to passenger domains of other autotransporter proteins, whereas the C-terminal portion of MapA resembled the translocation domain of conventional autotransporters. Cloning and expression of the M. catarrhalis mapA gene in Escherichia coli confirmed the presence of acid phosphatase activity in the MapA protein. The MapA protein was shown to be localized to the outer membrane of M. catarrhalis and was not detected either in the soluble cytoplasmic fraction from disrupted M. catarrhalis cells or in the spent culture supernatant fluid from M. catarrhalis. Use of the predicted MapA translocation domain in a fusion construct with the passenger domain from another predicted M. catarrhalis autotransporter confirmed the translocation ability of this MapA domain. Inactivation of the mapA gene in M. catarrhalis strain O35E reduced the acid phosphatase activity expressed by this organism, and this mutation could be complemented in trans with the wild-type mapA gene. Nucleotide sequence analysis of the mapA gene from six M. catarrhalis strains showed that this protein was highly conserved among strains of this pathogen. Site-directed mutagenesis of a critical histidine residue (H233A) in the predicted active site of the acid phosphatase domain in MapA eliminated acid phosphatase activity in the recombinant MapA protein. This is the first description of an autotransporter protein that expresses acid phosphatase activity.

The effects of external pH, temperature, and substrate concentration on acid phosphatase activity of ectomycorrhizal fungi

1986 ◽  
Vol 64 (11) ◽  
pp. 2383-2387 ◽  
Author(s):  
Robert K. Antibus ◽  
Carolyn J. Kroehler ◽  
Arthur E. Linkins
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Substrate Concentration ◽  
Acid Phosphatase Activity ◽  
Axenic Culture ◽  
Temperature Acclimation ◽  
Phenotypic Change ◽  
Acid Phosphatases ◽  
Cenococcum Geophilum

Isolates of the ectomycorrhizal fungi Cenococcum geophilum, Hebeloma pusillum, and Entoloma sericeum were grown in axenic culture to study the effects of assay pH, temperature, and substrate concentration on the activity of surface acid phosphatases. In addition, isolates were grown at 12 and 20 °C to determine whether the Arrhenius activation energies of surface phosphatases were affected by temperature acclimation. Four of the six isolates examined demonstrated distinct pH optima at pH 5.0; one isolate showed optimal activity at pH 4.5. None of the fungi examined produced significant surface alkaline phosphatase activity. Arrhenius activation energy values were not affected by lowering the growth temperature, suggesting that a phenotypic change in surface acid phosphatases did not occur with acclimation. Vmax and Km values for the hydrolysis of p-nitrophenyl phosphate were found to differ significantly among the isolates examined. Our findings support previous research by confirming the existence of interspecific and intraspecific differences in acid phosphatase activity, but they demonstrate the importance of considering assay pH and substrate concentration when making such comparisons.

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