Inorganic phosphate accumulation and phosphatase activity in the nucleus of maize embryo root cells

1981 ◽  
Vol 47 (1) ◽  
pp. 77-89
Author(s):  
R. Deltour ◽  
S. Fransolet ◽  
R. Loppes
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Inorganic Phosphate ◽  
Specific Activity ◽  
Ultrastructural Localization ◽  
High Concentration ◽  
Root Cells ◽  
Phosphatase Activities ◽  
Root Tissues

The nucleus of growing root cells Zea mays contains a high concentration of inorganic phosphate. In order to verify whether this high nuclear Pi concentration is correlated with the metabolic activity of the nucleus, the Pi has been visualized in root cells of maize embryos at the electron-microscope level during 2 different periods which are both characterized by a spectacular reactivation of the nuclear metabolism, i.e. the early germination and the period of recovery following a thermal treatment given to the seeds after 48 h of germination. In both situations the Pi concentration increased in the nucleus during its reactivation. To verify whether the high nuclear Pi concentration could be of endogenous origin, the phosphatase activities were measured in crude extracts of root tissues during nuclear reactivation. The specific activity was optimal at pH 4.5 and was shown to increase with cellular reactivation. The ultrastructural localization of acid phosphatase activity showed that Pi may be produced at 3 distinct sites: plasmalemma, vacuoles and most probably nucleus itself. High acid phosphatase activities were found in nuclei displaying a high metabolism. Taking these results and previous data into account, we suggest that a correlation may exist between the rate of nuclear transcription, the level of nuclear acid phosphatase activity and the nuclear Pi accumulation.

EFFECTS OF 5α-ANDROSTANE-3β,17β-DIOL AND 5β-DIHYDROTESTOSTERONE ON ACID PHOSPHATASE ACTIVITY IN THE PROSTATE GLAND OF THE CASTRATED ADULT RAT

1978 ◽  
Vol 79 (1) ◽  
pp. 9-16 ◽  
Author(s):  
M. P. TENNISWOOD ◽  
PAMELA P. ABRAHAMS ◽  
C. E. BIRD ◽  
A. F. CLARK
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Prostate Gland ◽  
Intraperitoneal Administration ◽  
Adult Rat ◽  
Secretory Acid Phosphatase

Polyacrylamide gel electrophoresis of filtrates from adult rat prostatic tissue showed two bands of acid phosphatase activity. These corresponded to the lysosomal and secretory acid phosphatases. After castration the secretory acid phosphatase disappeared. The specific activity of the enzyme increased from the time of castration to a maximum on day 7 before declining steadily, while the percentage inhibition by tartrate of acid phosphatase increased from control levels to a maximum on day 7 and then decreased to a new steady state by day 15. When 5α-androstane-3β,17β-diol was administered i.p. at a dose of 2 mg/day, starting immediately after castration, the secretory acid phosphatase was retained but the percentage inhibition and the specific activity were both raised above control levels. When this steroid was administered daily starting 7 days after castration the secretory acid phosphatase band on the gels returned more rapidly than with the classical androgens, but the percentage inhibition and specific activity were once again raised. Intraperitoneal administration of 5β-dihydrotestosterone, at a dose of 2 mg/day, did not maintain the secretory acid phosphatase activity which disappeared by day 5. However, the specific activity of acid phosphatase and the percentage inhibition by tartrate were both raised throughout the experiment. If this steroid was given 7 days after castration, the percentage inhibition by tartrate did not respond and fell to the level seen in castrated rats. The specific activity, however, remained significantly above the level found in castrated control rats.

Kinetic Method for Determining Acid Phosphatase Activity in Serum with Use of the "CentrifiChem"

1972 ◽  
Vol 18 (8) ◽  
pp. 841-844 ◽  
Author(s):  
Diane L Fabiny-Byrd ◽  
Gerhard Ertingshausen
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Kinetic Method ◽  
Reaction Rates ◽  
Phosphatase Activities ◽  
Fast Red ◽  
Presence And Absence

Abstract Acid phosphatase activity is determined by splitting 1-naphthyl phosphate, concurrently diazotizing the released 1-naphthol with Fast Red TR, and measuring the resulting color. The test is performed in the presence and absence of tartrate. Reaction rates can be continuously monitored, and their difference is proportional to acid phosphatase activity that is inhibited by tartrate. Results for sera with normal and increased acid phosphatase activities are presented and three different methods for acid phosphatase are compared. The kinetic blank used in the reaction eliminates all nonenzymatic contributions to substrate splitting.

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.

Acid phosphatase activity in Pinus pinea – Tuber albidum ectomycorrhizal association

1992 ◽  
Vol 70 (7) ◽  
pp. 1377-1383 ◽  
Author(s):  
S. Pasqualini ◽  
F. Panara ◽  
M. Antonielli
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Middle Lamella ◽  
Ultrastructural Localization ◽  
Ectomycorrhizal Fungus ◽  
Pinus Pinea ◽  
Inorganic Pyrophosphate ◽  
Mycorrhizal Roots ◽  
Substrate Concentrations

Acid phosphatase activity of pine (Pinus pinea L.) roots was investigated in the presence or absence of the ectomycorrhizal fungus Tuber albidum Pico. Acid phosphatase activity was higher in mycorrhizal roots than in roots of uncolonized control plants. The optimum pH values for acid phosphatase were 3.5 and 5.0 for mycorrhizal roots and 5.0 for control roots. The acid phosphatase activity was inhibited by tartrate, fluoride, and molybdate ions, but a lower inhibition was exerted by orthophosphate. Mycorrhizal roots of pine possessed active acid phosphatases that hydrolyzed a wide variety of natural and synthetic phosphate esters. In particular, the enzyme was active against phytate and inorganic pyrophosphate. Two different Km values were estimated: about 0.22 mM and 2.78 mM at low and high substrate concentrations, respectively. The ultrastructural localization of acid phosphatase in mycorrhizal roots showed that the activity in the Hartig net was mainly localized in the plasmalemma of hyphae. Some lead phosphate precipitates were also observed in the middle lamella of the host cell. Key words: Pinus pinea, Tuber albidum, acid phosphatase, ectomycorrhiza, histochemical localization.

Soil enzyme activities following paper sludge addition in a winter cabbage-sweet corn rotation

2000 ◽  
Vol 80 (1) ◽  
pp. 91-97 ◽  
Author(s):  
B. Gagnon ◽  
R. Lalande ◽  
R. R. Simard ◽  
M. Roy
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Sweet Corn ◽  
Soil Enzyme ◽  
Phosphatase Activities ◽  
Arylsulfatase Activity ◽  
Papermill Sludge ◽  
Soil Acid Phosphatase

Combined primary and secondary papermill sludge (PS) is a good source of C and other nutrients for soils devoted to intensive horticultural production. A field study was conducted to evaluate the effect of PS, spring-applied alone or in combination with ammonium nitrate (AN), on the enzymatic activity of a Bedford clay (Humic Gleysol) in the province of Québec, Canada. The experiment was started in 1996 with winter cabbage (Brassica oleracea var. capitata L.) and continued in 1997 and 1998 on the same plots with sweet corn (Zea mays L.). The PS was applied at 0 (control), 8, 16, 32 and 65 Mg ha−1 in 1996 and at 44% of these rates in 1997. No sludge was applied in 1998. Additional treatments consisted of AN applied yearly at 100% of the plant N requirements and a PS and AN combination. Soil arylsulfatase and acid and alkaline phosphatase activities were measured at three different times in each growing season. The PS rate linearly increased the soil acid phosphatase activity in all 3 yr. In contrast, the alkaline phosphatase and arylsulfatase activities were enhanced in 1997 by the 8–16 Mg PS ha−1 treatments, whereas larger amounts of PS showed activity comparable to the control. The second PS application promoted phosphatase activities mostly in fall, but did not sustain arylsulfatase activity. The AN gave lower phosphatase activities than PS, and depressed arylsulfatase. Addition of AN to PS increased only acid phosphatase activity as compared with PS alone or the control. This study indicated that addition of PS improved enzyme activity of this horticultural soil but rates in excess to 32 Mg ha−1 may be detrimental. Key words: Papermill sludge, soil enzyme, cabbage, corn

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.

Intraspecific genetic variation of acid phosphatase activity in monokaryotic and dikaryotic populations of the ectomycorrhizal fungus Hebeloma cylindrosporum

1991 ◽  
Vol 69 (4) ◽  
pp. 808-813 ◽  
Author(s):  
J. P. Meysselle ◽  
G. Gay ◽  
J. C. Debaud
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Specific Activity ◽  
Intraspecific Variability ◽  
Ectomycorrhizal Fungus ◽  
Hebeloma Cylindrosporum ◽  
Single Strain ◽  
Wild Strains

Intraspecific variability of acid phosphatase activity and mycelial growth of the ectomycorrhizal fungus Hebeloma cylindrosporum Romagnesi was examined because of the role of this enzyme activity in the phosphate nutrition of the fungus and consequently of mycorrhizal host plants. Interstrain variation was studied with 11 wild strains, and intrastrain variability was studied with 20 sib-monokaryons and 50 reconstituted dikaryons, progeny of the HC1 fruiting strain. The range of variation of acid phosphatase activity among wild dikaryotic mycelia was the same as that among sib-monokaryons or dikaryons belonging to the progeny of a single strain. The total phosphatase activity of the wild strains ranged from 5.70 to 96.0 total milliunits (TmU). It ranged from 11.1 to 120.5 TmU within sib-monokaryons and from 34.2 to 178.1 TmU for reconstituted dikaryons. Specific phosphatase activity of wild dikaryons ranged from 48.5 international milliunits (ImU) to 675.6 ImU, whereas the ranges of variation among sib-monokaryons and reconstituted dikaryons were, respectively, 85.3–791.0 and 270.7–816.1 ImU. On average, sib monokaryons and reconstituted dikaryons had lower activity than their parental dikaryon. However, four reconstituted dikaryons had a higher specific activity than the original dikaryon HC1. The growth of the studied mycelia also varied, but in a narrower range (from 97.1 to 151.6 μg protein per culture for wild dikaryons, from 130.1 to 199.1 μg for sib-monokaryons, and from 160.6 to 275.9 μg for reconstituted dikaryons). No correlation could be detected between specific acid phosphatase activity and growth rate in pure culture within the different monokaryotic or dikaryotic populations studied. These results demonstrate the possibility of obtaining, by intrastrain crossings, mycelia having higher phosphatase activity than the parental wild strains. The characteristics of the different mycelia are discussed in relation to a selection program and their putative spatial distribution in natural conditions. Key words: acid phosphatase, ectomycorrhizal fungus, intraspecific variation, monokaryon, dikaryon, Hebeloma cylindrosporum.

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.

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