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.

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.

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.

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.

scholarly journals The effect of water and salt stresses on the phosphorus content and acid phosphatase activity in oilseed rape

2014 ◽  
Vol 58 (1) ◽  
pp. 47-57 ◽  
Author(s):  
Stanisław Flasiński ◽  
Ryszard Zamorski ◽  
Urszula Kotowska
Keyword(s):  
Enzyme Activity ◽  
Salt Stress ◽  
Acid Phosphatase ◽  
Water Stress ◽  
Plant Growth ◽  
Phosphatase Activity ◽  
Oilseed Rape ◽  
Acid Phosphatase Activity ◽  
Phosphorus Content ◽  
Young Leaves

Oilseed rape plants responded to water and salt stresses (-0.5 MPa, PEG 6000 and NaCI) by reduction of the fresh and dry weights of shoots and roots. When PEG was used, the ratio of dry weights of roots:shoots surpassed that of controls. The leaf protein content increased considerably. The phosphorus content decreased only in the roots, most significantly after three days of stress. Immediately after the stresses were induced, an increase in the acid phosphatase (AP) activity was noted. Water and salt stresses caused four- and two-fold increases in AP activity in leaves, respectively. Changes in the enzyme activity were negligible in stems and roots. There are nine forms of AP in young leaves of oilseed rape. In the stressed plants, from No. 5 revealed lower activity and forms Nos 8 and 9, higher activities than in the control. The increase in AP activity was directly accompanied by the decrease in the water potential of the tissues. Oilseed rape is considerably less sensitive to salt stress than to water stress, which is manifested as the lower inhibition of plant growth and also by a smaller increase in acid phosphatase activity.

Significance of "high" acid phosphatase activity in the serum of normal children.

1979 ◽  
Vol 25 (5) ◽  
pp. 719-722 ◽  
Author(s):  
J Chen ◽  
L T Yam ◽  
A J Janckila ◽  
C Y Li ◽  
W K Lam
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Giant Cells ◽  
Tartrate Resistant Acid Phosphatase ◽  
Giant Cell Tumors ◽  
Normal Children ◽  
Age Related ◽  
Normal Adults

Abstract Serum acid phosphatase activity in normal children (newborn to 18 years) is several fold that in normal adults. Activity is age-related but not sex-related. The isoenzyme pattern in children is similar to that in adults and contains no prostatic fraction. Quantitatively, most of the enzyme activity in the serum of children is tartrate-resistant and correlates well with heat-labile fractions of alkaline phosphatase activity in serum, suggesting that the source of the higher acid phosphatase activity in children is bone. Significant tartrate-resistant acid phosphatase activity was demonstrated in the giant cells in three patients with giant-cell tumors, but not in the "osteoblasts" in six patients with osteogenic sarcomas and many other normal or abnormal tissues. This work suggests that the higher enzyme activity in the serum of children represents a normal physiological phenomenon resulting from their greater osteoclastic activity.

Effects of physiological concentrations of parathyroid hormone on acid phosphatase activity in cultured rat bone cells

1986 ◽  
Vol 111 (1) ◽  
pp. 17-26 ◽  
Author(s):  
I. P. Braidman ◽  
J. G. St John ◽  
D. C. Anderson ◽  
W. R. Robertson
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
B Cells ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Bone Cells ◽  
Cell Populations ◽  
C Cells ◽  
C Cell ◽  
Type C

ABSTRACT The mechanism by which parathyroid hormone (PTH) induces osteoclastic bone resorption is still incompletely understood. Recent evidence suggests that the hormone exerts its effects indirectly, via the osteoblasts. Bone cells isolated from fetal rat calvaria by enzymatic digestion were used. Two heterogeneous cell populations were isolated by equilibrium density centrifugation on Percoll gradients and maintained by differential culture conditions. These two populations, which are morphologically distinguishable from one another by light and electron microscopy, have been characterized previously both biochemically and with regard to their hormonal (PTH and calcitonin) responses. We have called them type C cells (containing cells with some of the properties of osteoclasts) and type B cells (containing osteoblast-like cells, as well as fibroblasts, chondrocytes and other stromal cells). In the present study, we have further characterized the functional relationship between the two cell populations, with particular regard to the hormonal responses of type C cultures. Acid phosphatase, measured cytochemically in individual cells, was used as a marker for C cell responses. C cells had significantly higher levels of acid phosphatase activity than either B cells or spleen macrophages. Calcitonin (0–10 pg/ml) decreased C cell acid phosphatase activity but was without effect on B cells or spleen macrophages. Co-culture of C cells with B cells produced increased enzyme activity only in the former; this effect could be mimicked if fibroblasts replaced B cells and cell contact was essential for this response. PTH (0–10 pg/ml) raised enzyme activity further in C cells only when they were cultured with B cells. When C cells were cultured so that they shared medium, but were not in contact, with B cells, PTH (2 pg/ml) still increased enzyme activity in the former. Fibroblasts were ineffective in this system. Spleen macrophages were also unresponsive to PTH when substituted for C cells. Calcitonin (10 pg/ml) blocked the effects of PTH on C cells. These results indicate that macrophages are probably not a significant proportion of the C cell population, and that PTH may produce increased acid phosphatase activity in C cells via a humoral factor produced by cells present in B cell cultures. J. Endocr. (1986) 111, 17–26

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