scholarly journals Heterogeneity of liver acid phosphatases in developing chick embryo

1969 ◽  
Vol 115 (2) ◽  
pp. 191-197 ◽  
Author(s):  
K.-M. Wang
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Soluble Fraction ◽  
The Other ◽  
Acid Phosphatases ◽  
Peak Activity ◽  
Ph Optimum ◽  
Triton X ◽  
Soluble Fractions

1. The development, localization and heterogeneity of acid phosphatase and a Zn2+-activated acid phosphatase in cellular fractions of developing chick liver were studied. 2. Acid phosphatase is distributed abundantly in the particulate and soluble fractions. The soluble fraction is rich in Zn2+-activated acid phosphatase, which attains its peak activity at about 15 days of incubation. 3. The particulate acid phosphatase activity is inhibited by fluoride but not by sodium l(+)-tartrate or cysteine. On the other hand, the soluble Zn2+-activated acid phosphatase activity is inhibited by sodium l(+)-tartrate and cysteine but not by fluoride. 4. The pH optimum of these two enzymes is similar at about 5·6. 5. The soluble Zn2+-activated acid phosphatase activity appears to be thermally stabilized by the treatment with Triton X-100 or bovine serum albumin.

scholarly journals ISOZYMES OF ACID PHOSPHATASE IN NORMAL AND CALMETTE-GUÉRIN BACILLUS-INDUCED RABBIT ALVEOLAR MACROPHAGES

1968 ◽  
Vol 128 (5) ◽  
pp. 1031-1048 ◽  
Author(s):  
S. G. Axline
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alveolar Macrophages ◽  
Acid Phosphatase Activity ◽  
Enzyme Inhibitors ◽  
Freezing And Thawing ◽  
Ph Optimum ◽  
Lysosomal Fraction ◽  
Repeated Freezing ◽  
Major Acid

The acid phosphatase activity of normal alveolar and BCG-induced alveolar macrophages has been examined. Five electrophoretically distinct forms of acid phosphatase have been identified in both normal and BCG-induced macrophages. The acid phosphatases can be divided into two major categories. One category, containing four distinct forms, is readily solubilized after repeated freezing and thawing or mechanical disruption The second category, containing one form, is firmly bound to the lysosomal membrane and can be solubilized by treatment of the lysosomal fraction with Triton X-100. The Triton-extractable acid phosphatase and the predominant aqueous soluble acid phosphatase have been shown to differ in the degree of membrane binding, in solubility, in net charge, and in molecular weight. The two pre-dominant phosphatases possess identical pH optimum and do not differ in response to enzyme inhibitors. BCG stimulation has been shown to result in a nearly twofold increase in acid phosphatase activity. A nearly proportionate increase in the major acid phosphatase forms has been observed.

Acid Phosphatase Activity in Vegetative Cells and Spores of Clostridium botulinum Type E

1971 ◽  
Vol 28 (11) ◽  
pp. 1817-1820 ◽  
Author(s):  
G. A. Strasdine ◽  
Joanne M. Melville
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Clostridium Botulinum ◽  
Specific Activity ◽  
Growth Media ◽  
Ph Optimum ◽  
Vegetative Cells ◽  
Botulinum Type ◽  
Clostridium Botulinum Type E

Acid phosphatase activity with a pH optimum of 5 was demonstrated in vegetative cells, spores, and germinated spores of Clostridium botulinum type E (Minnesota). The enzyme was present in the cells during all stages of growth and was insensitive to the orthophosphate concentration of the growth media. Specific activity of the enzyme increased during growth coincident with a loss in inorganic phosphate from the acid-soluble cell fraction. Magnesium or manganese was required for maximum enzyme activity. Acid phosphatase in crude spore extracts was more heat-stable than in extracts obtained from vegetative cells.

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.

Acid Phosphatase Activities in Developing Seeds of Pisum sativum L

1977 ◽  
Vol 4 (6) ◽  
pp. 843 ◽  
Author(s):  
DR Murray ◽  
MD Collier
Keyword(s):  
Acid Phosphatase ◽  
Pisum Sativum ◽  
Phosphatase Activity ◽  
Cell Expansion ◽  
Acid Phosphatase Activity ◽  
Minor Components ◽  
Ph Optimum ◽  
Pisum Sativum L ◽  
Almost All ◽  
Pea Seed

The seedcoats contain almost all of the acid phosphatase activity (EC 3.1.3.2) in the pea seed in the earliest stages of expansion. The seedcoat activity is maximal by the end of the period of rapid cell expansion and declines as the embryo matures. The developing cotyledons show a later rise in acid phosphatase activity to a maximum shortly before dehydration. The activity in the embryonic axis shows a marked increase only during dehydration. The acid phosphatase activity in the seedcoats results almost entirely from an isoenzyme with high electrophoretic mobility in 5.5% polyacrylamide gels (RF 0.97). This isoenzyme has not been detected in other tissues from the plant. The phosphatase activity in the cotyledons is accounted for by one major isoenzyme at RF 0.75 and by four minor components. The partially purified enzyme from the seedcoats shows a broad pH optimum from pH 5.0 to pH 6.0. In contrast, the preparation from the cotyledons has an optimum close to pH 5.6 and is slightly more sensitive to inhibition by 0.2 mM PI.

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 DEMONSTRATION OF ACID PHOSPHATASE ACTIVITY USING 1-ACETYL-3-INDOLYL PHOSPHATE AS SUBSTRATE

1971 ◽  
Vol 19 (3) ◽  
pp. 175-181 ◽  
Author(s):  
MASANDO HAYASHI
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Lead Ions ◽  
Lead Salt ◽  
Male Rats ◽  
Cytochemical Demonstration ◽  
Liver And Kidney ◽  
Triton X

A simultaneous coupling azo-indoxyl method for the cytochemical demonstration of acid phosphatase activity using p-toluidine salt of 1-acetyl-3-indolyl phosphate is described. A satisfactory staining for the enzyme activity was obtained following incubation of formol-calcium-fixed frozen sections for 30 min at 25°C in a medium containing 1 mM each of the substrate and hexazonium pararosanilin and adjusted to pH 4.5-5.0 with acetate buffer. The distribution of acid phosphatase activity demonstrated by this method was identical with that obtained either by Gomori's technique using β-glycerophosphate as substrate or by the Barka and Anderson's naphthol AS-BI phosphate-hexazonium pararosanilin method in several tissues of male rats so far examined. However, the adrenal enzyme activity was most prominent in the medulla with 1-acetyl-3-indolyl phosphate and β-glycerophosphate but it was more marked in the cortex with naphthol AS-BI phosphate. An advantage of using 1-acetyl-3-indolyl phosphate as substrate is that the same compound can be used for comparing azo-indoxyl and lead-salt methods. Effects of phospholipase C and Triton X-100 on staining for acid phosphatase were tested by pretreating fixed rat liver and kidney sections with these agents and incubating them in the medium containing 1-acetyl-3-indolyl phosphate and either hexazonium pararosanilin or lead ions as a coupler. The pretreatment did not change discrete lysosomal staining, as seen in untreated controls, using pararosanilin as a coupler, but greatly modified the staining using lead ions. The results indicate that the preciseness of staining for acid phosphatase with lead-salt method is highly dependent on some lipid material which attracts lead in tissues and that appropriately devised azo dye or azo-indoxyl methods demonstrate enzyme sites more accurately than lead-salt method.

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.

Variation in acid phosphatase activity among progeny from controlled crosses in the ectomycorrhizal fungus Laccaria bicolor

1990 ◽  
Vol 68 (4) ◽  
pp. 864-866 ◽  
Author(s):  
Bradley R. Kropp
Keyword(s):  
Acid Phosphatase ◽  
Key Words ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Ectomycorrhizal Fungus ◽  
The Other ◽  
Laccaria Bicolor ◽  
Polygenic Inheritance ◽  
Controlled Crosses

The variation in acid phosphatase activity among the monokaryotic F1 progeny from two different synthesized dikaryotic cultures of the ectomycorrhizal basidiomycete Laccaria bicolor was examined. The progeny of one of the dikaryons showed variation in acid phosphatase activity up to 10 times that of the lowest value. The progeny of the other dikaryon were much less variable, showing differences of up to 5 times the lowest value. Both sets of monokaryotic progeny showed distributions indicative of polygenic inheritance for acid phosphatase activity in this fungus. Key words: ectomycorrhizae, genetics, monokaryon, acid phosphatase, Laccaria bicolor.

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