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.

HYDROLYZING ENZYME ACTIVITY IN THE BRAIN AND THE RETROCEREBRAL SYSTEM OF THE AMERICAN COCKROACH (PERIPLANETA AMERICANA (L)) WITH SPECIAL REFERENCE TO THE NEUROSECRETORY MATERIALS

1964 ◽  
Vol 42 (2) ◽  
pp. 281-293 ◽  
Author(s):  
Y. Y. Shao ◽  
S. E. Dixon
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Periplaneta Americana ◽  
American Cockroach ◽  
Soluble Form ◽  
Neurosecretory System ◽  
Acid Phosphatases ◽  
The Brain

Some hydrolyzing enzymes have been investigated by histochemical and biochemical methods. Almost all neurons in the brain contain acid phosphatases. About half of the total activity is associated with subcellular particles. Most of the acid-phosphatase activity in the corpora cardiaca (CC) is associated with the neurosecretory materials (NSM). Elementary neurosecretory granules (ENG) have been isolated from the CC by fractionation and subfractionation procedures and subjected to in vitro enzyme activity studies. Electron micrographs of the subfraction having the highest acid-phosphatase activity are discussed in relation to three types or "stages" of ENG. About 80% of the total esterase activity in the brain and the retrocerebral system has been found to be in a "soluble" form. The remaining 20%, the "insoluble" forms, may be associated with subcellular organelles. The methods of Gomori and Burstone for acid-phosphatase localizations are compared, and differing results discussed. The possible roles or functions of acid phosphatases and esterases in the neurosecretory system are discussed.

Acid phosphatase, alkaline phosphatase, and nitrate reductase activity of selected ectomycorrhizal fungi

1989 ◽  
Vol 67 (3) ◽  
pp. 750-753 ◽  
Author(s):  
Iwan Ho
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Nitrate Reductase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Phosphatase Alkaline

Seventeen isolates, encompassing five genera and eight species of ectomycorrhizal fungi, were compared for acid phosphatase, alkaline phosphatase, and nitrate reductase activity. Isolates within species differed in enzyme activity and isozyme patterns by host specificity and site (as exemplified by the genus Suillus). Host and site may have affected phosphatase enzyme activity. Generally, the Douglas-fir associates, which dominate in mesic sites, have higher acid phosphatase activity than pine associates, which mostly occupy xeric sites; however, pine associates from mesic sites also have higher acid phosphatase activity (e.g., S. tomentosus). In four isolates of Amanita muscaria, the effect of site was also apparent. Two of them, which have significantly higher acid phosphatase activity than the others, were isolated from mesic sites. The isozyme pattern of the genus Suillus appeared to be separated by host groups. Other isolates with only one species also differed more or less by host groups. They shared at least one band within host groups, except for the two isolates of Paxillus involutus from different hosts. The P. involutus S-403 isolated from an orchard showed much higher nitrate reductase activity than all other isolates. No apparent differences in nitrate reductase activity were found between the other isolates.

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.

scholarly journals Croatian produced unifloral honey characterized according to the protein and proline content and enzyme activities

2016 ◽  
Vol 60 (1) ◽  
pp. 39-48 ◽  
Author(s):  
Ivana Flanjak ◽  
Ivica Strelec ◽  
Daniela Kenjerić ◽  
Ljiljana Primorac
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Protein Content ◽  
Glucose Oxidase ◽  
Phosphatase Activity ◽  
Enzyme Activities ◽  
Acid Phosphatase Activity ◽  
Black Locust ◽  
Proline Content ◽  
A Minor

Abstract In honey, the content of proteins, including the enzymes, is relatively low and has a minor nutritive significance. On the other hand, the proteins, including the enzymes, are usually used as honey quality evaluation parameters. This is because protein content and enzyme activities vary regarding the botanical origin of the honey. Since the results of protein content, glucose-oxidase, and acid phosphatase, for honeys produced in Croatia, are not available, four of the most abundant honey types produced in Croatia (black locust, sage, chestnut, and honeydew honey) are characterised according to the protein and proline content and enzyme activities. The characterisation was done to determine specificities and contribute to the characterisation of unifloral honeys. Dark honey types (honeydew and chestnut honey) had a higher proline content, and diastase, invertase, and glucose-oxidase activity than lighter sage and black locust honey. Black locust honey has a naturally low enzyme activity and showed the highest acid phosphatase activity among the analysed honey types, while honeydew honey, otherwise known to possess high proline content and enzyme activity, had a low protein content comparable to black locust honey. Statistically significant correlations were obtained between all analysed parameters, with the exception of acid phosphatase activity.

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 PURIFICATION OF GLUTARALDEHYDE ITS SIGNIFICANCE FOR PRESERVATION OF ACID PHOSPHATASE ACTIVITY

1968 ◽  
Vol 16 (3) ◽  
pp. 199-204 ◽  
Author(s):  
H. DARIUSH FAHIMI ◽  
PIERRE DROCHMANS ◽  
A. POPOWSKI
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Phosphatase Activity ◽  
Rat Liver ◽  
Acid Phosphatase Activity ◽  
High Concentration ◽  
Liver Homogenates ◽  
Inorganic Phosphates

The inhibition of acid phosphatase activity in rat liver homogenates after fixation in different lots of commercial glutaraldehyde is determined and compared with the inhibition following fixation with a distilled product. It is shown that commercial glutaraldehydes inhibit more of the enzyme activity than the distilled product. The acidic products of oxidation of glutaraldehyde do not increase the inhibition of the enzymatic activity. The presence of high concentration of inorganic phosphates in different lots of commercial glutaraldehyde, as presented here, suggests that probably such impurities may be responsible for increased inhibition of phosphatase activity noted after fixation in commercial glutaraldehydes.

Acid phosphatase activity in maize (Zea mays La) seedlings treated with sodium humate

2014 ◽  
Vol 55 (2) ◽  
pp. 181-188 ◽  
Author(s):  
Marie Kummerova ◽  
Vladimir Tichy
Keyword(s):  
Zea Mays ◽  
Enzyme Activity ◽  
Free Radicals ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Sodium Humate ◽  
Humus Substances ◽  
Unfavourable Effect ◽  
Fraction I

Sodium humate increased the acid phosphatase activity of fraction II of imbibing maize caryopses and suppressed the enzyme activity in fraction I. Removal of the testa changed the stimulating action of humate on the acid phosphatase activity of fraction II into an inhibiting one and intensified its unfavourable effect on this enzyme's activity in fraction l. Sodium humate inhibited the acid phosphatase activity of this fraction from both leaves and roots. The results obtained are in agreement with the theory of free radicals of humus substances being involved in action on biuecmbranes.

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