Localisation cytochimique des activités phosphatasiques acides de champignons mycorhiziens développés sur milieu complet ou carencé en phosphate

1983 ◽  
Vol 61 (5) ◽  
pp. 1411-1414 ◽  
Author(s):  
Bernadette Lacaze
Keyword(s):  
Electron Microscopy ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Cell Walls ◽  
Acid Phosphatase Activity ◽  
Inorganic Phosphate ◽  
Light And Electron Microscopy ◽  
Reaction Products ◽  
Cytochemical Study

The mycelia of three mycorrhizal basidiomycètes (Pisolithus tinctorius (Pers.) Coker et Couch., Suillus granulatus (L. ex Fr.) O. Kuntze and S. bellinii (Izenga) Watling) were grown on media with or without inorganic phosphate. A cytochemical study of the distribution of acid phosphatase activity was made using light and electron microscopy. Highly enhanced enzyme activity was observed in the phosphorus-deficient mycelia. Precipitates were located primarily at the surface of the fungal cells. Cell walls appear devoid of reaction products in most cases.

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.

Parallel Intralysosomal Amyloid Fibrils, a Possible Result of Phagocytosis

1977 ◽  
Vol 14 (4) ◽  
pp. 407-419 ◽  
Author(s):  
E. Gruys ◽  
M. Castaño
Keyword(s):  
Electron Microscopy ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Enzyme Histochemistry ◽  
Amyloid Fibrils ◽  
Light And Electron Microscopy ◽  
Interstitial Cells ◽  
Mesenchymal Cells ◽  
Parallel Arrangement

Vacuoles of mesenchymal cells in the papillae of bovine kidneys with amyloidosis were studied by histochemical electron microscopy for acid phosphatase as a marker for lysosomes. The vacuoles contained parallel amyloid fibrils. The vacuoles of reticular interstitial cells were found to be lysosomes. Vacuoles of macrophage-like cells of the same papillae were positive, partially positive, or negative for the enzyme activity. A suspension of papillary material was injected subcutaneously in rats in a 21-day light and electron microscopy and enzyme histochemistry study. Amyloid was demonstrated in vacuoles of macrophages throughout this period and initially also in neutrophils. In most vacuoles amyloid fibrils were randomly arranged but in others parallel arrangement was demonstrated. Amyloid was only at the inoculation sites. Intralysosomal bovine amyloid may occur in parallel fibrillar arrangement without a definite indication for amyloid production.

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.

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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