Localization of acid phosphatase activity in the apoplast of pea (Pisum sativum L.) root nodules grown under phosphorus deficiency

2006 ◽  
Vol 28 (3) ◽  
pp. 263-271 ◽  
Author(s):  
Marzena Sujkowska ◽  
Wojciech Borucki ◽  
Władysław Golinowski
Keyword(s):  
Acid Phosphatase ◽  
Pisum Sativum ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Root Nodules ◽  
Phosphorus Deficiency ◽  
Pisum Sativum L

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.

Effects of Cytochalasin B on germinating seeds of Pisum sativum L. Respiration, ultrastructure of cotyledonary cells, storage substances, acid phosphatase activity

1983 ◽  
Vol 117 (5-6) ◽  
pp. 227-236 ◽  
Author(s):  
Raffaella Preziosi Tamagnini ◽  
Bruno Romano ◽  
Giuseppe Frenguelli ◽  
Anna Maria Bisogni
Keyword(s):  
Acid Phosphatase ◽  
Pisum Sativum ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Cytochalasin B ◽  
Pisum Sativum L ◽  
Germinating Seeds

Localization of acid phosphatase activity in maize root under phosphorus deficiency

1986 ◽  
Vol 28 (4) ◽  
pp. 270-274 ◽  
Author(s):  
Marie Kummerová
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Phosphorus Deficiency ◽  
Maize Root

Effects of drought, aging and phosphorus status on leaf acid phosphatase activity in wheat

1984 ◽  
Vol 35 (6) ◽  
pp. 777 ◽  
Author(s):  
KD McLachlan
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Total Phosphorus ◽  
Acid Phosphatase Activity ◽  
Phosphorus Deficiency ◽  
Moisture Stress ◽  
Inorganic Phosphorus ◽  
Plant Age ◽  
Phosphorus Concentration ◽  
Total Phosphorus Concentration

Wheat plants grown at two levels of phosphorus supply were subjected to drought or given adequate water. Acid phosphatase activities in the youngest fully expanded leaves, and inorganic and total phosphorus concentrations in the plant tops were determined at four stages of crop development. Phosphatase activity increased with plant age, with phosphorus deficiency and with drought. Inorganic phosphorus concentration decreased with plant age and phosphorus deficiency. Drought markedly decreased the inorganic phosphorus concentration in phosphorus sufficient plants but had little effect on the concentration in deficient plants. Total phosphorus concentration increased as the plants aged and was greatest where the plants were phosphorus sufficient and adequately watered. Drought markedly reduced the total phosphorus concentration in phosphorus sufficient plants, but had little effect on the total phosphorus concentration in deficient plants. Leaf acid phosphatase activity was related inversely to the inorganic phosphorus concentration in the plant tops. Changes in activity with aging, phosphorus supply and moisture stress were associated with changes in the inorganic phosphorus concentration. An argument is developed which indicates that a single 'critical value' separating sufficient from deficient plants, either for phosphatase activity, inorganic or total phosphorus concentration, is not practicable. Different values will be required for different stages of maturity. Complications introduced by drought and aging, through their effect on phosphorus concentration and enzyme activity, were overcome by developing phosphatase zymograms. Two bands were specifically associated with phosphorus deficient plants irrespective of plant age or moisture stress. The technique offers further opportunity for studies in phosphorus metabolism and shou!d provide a useful means of diagnosing phosphorus deficiency in field groRn plants.

Biomass partitioning and rhizosphere responses of maize and faba bean to phosphorus deficiency

2016 ◽  
Vol 67 (8) ◽  
pp. 847 ◽  
Author(s):  
Haitao Liu ◽  
Philip J. White ◽  
Chunjian Li
Keyword(s):  
Acid Phosphatase ◽  
Organic Acids ◽  
Phosphatase Activity ◽  
Faba Bean ◽  
Acid Phosphatase Activity ◽  
Phosphorus Deficiency ◽  
Water Soluble ◽  
Bulk Soil ◽  
Root Tips ◽  
P Supply

Maize (Zea mays L.) and faba bean (Vicia faba L.) have contrasting responses to low phosphorus (P) supply. The aim of this work was to characterise these responses with respect to the partitioning of biomass between shoot and root and biochemical modification of the rhizosphere. Maize and faba bean were grown in rhizoboxes in soil with a low P (10 mg kg–1) or high P (150 mg kg–1) supply. Solutions were collected from rhizosphere and bulk soil by suction, using micro-rhizons in situ. The pH and water-soluble P (Pi) were determined on the solutions collected by using micro-rhizons. Olsen P, soil pH and acid phosphatase activity were determined on samples of rhizosphere and bulk soil. Organic acids released from root tips were collected non-destructively and analysed by high performance liquid chromatography. Plants grown with low P supply had higher ratios of root : shoot dry weight than plants grown with high P supply. This response was greater in maize than in faba bean. Rhizosphere acidification, organic acid concentrations and acid phosphatase activity were greater in faba bean than maize. The Pi concentration in the maize rhizosphere solution was less than in the bulk soil, but the Pi concentration in the rhizosphere solution of faba bean was greater than in the bulk soil. It was concluded that maize responded to low P supply by investing more biomass in its root system, but acidification, concentrations of organic acids, acid phosphatase activity and mobilisation of P in the rhizosphere were greater in faba bean than in maize.

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

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