Variation in acid phosphatase activity among progeny from controlled crosses in the ectomycorrhizal fungus Laccaria bicolor

1990 ◽  
Vol 68 (4) ◽  
pp. 864-866 ◽  
Author(s):  
Bradley R. Kropp
Keyword(s):  
Acid Phosphatase ◽  
Key Words ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Ectomycorrhizal Fungus ◽  
The Other ◽  
Laccaria Bicolor ◽  
Polygenic Inheritance ◽  
Controlled Crosses

The variation in acid phosphatase activity among the monokaryotic F1 progeny from two different synthesized dikaryotic cultures of the ectomycorrhizal basidiomycete Laccaria bicolor was examined. The progeny of one of the dikaryons showed variation in acid phosphatase activity up to 10 times that of the lowest value. The progeny of the other dikaryon were much less variable, showing differences of up to 5 times the lowest value. Both sets of monokaryotic progeny showed distributions indicative of polygenic inheritance for acid phosphatase activity in this fungus. Key words: ectomycorrhizae, genetics, monokaryon, acid phosphatase, Laccaria bicolor.

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.

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.

Effects of Hebeloma arenosa and phosphorus fertility on root acid phosphatase activity of red pine (Pinus resinosa) seedlings

1991 ◽  
Vol 69 (2) ◽  
pp. 380-383 ◽  
Author(s):  
Janet MacFall ◽  
Steven A. Slack ◽  
Jaya Iyer
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Fungal Growth ◽  
Pinus Resinosa ◽  
Ectomycorrhizal Fungus ◽  
Red Pine ◽  
Nitrophenyl Phosphate

The ectomycorrhizal fungus Hebeloma arenosa Burdsall, MacFall & Albers was assayed for surface-accessible acid phosphatase activity in vitro on roots of red pine (Pinus resinosa Ait.) seedlings. Hebeloma arenosa was grown in defined liquid media containing 0, 17, 34, 68, or 136 mg/L phosphorus for 4 weeks. When assayed for acid phosphatase activity with p-nitrophenyl phosphate, 7.3 μmol of orthophosphate were released per gram dry weight of fungal tissue. There was no effect of added P on enzyme activity, excluding the treatment with no added P in which there was negligible fungal growth. Red pine seedlings were grown in Sparta loamy fine sand amended with 0, 17, 34, 68, or 136 mg/kg P as superphosphate, with and without H. arenosa inoculum. Mycorrhizal roots had greater enzyme activity than nonmycorrhizal roots of seedlings grown in similarly P-amended soil. This was determined by the following three assays: orthophosphate release from two salts of myoinosital hexaphosphate (Na and KMg) and from p-nitrophenyl phosphate. It is suggested that greater acid phosphatase activity by roots mycorrhizal with H. arenosa is one mechanism for improved P nutrition through the formation of a pool of P released from sources unavailable for direct intake.

scholarly journals Heterogeneity of liver acid phosphatases in developing chick embryo

1969 ◽  
Vol 115 (2) ◽  
pp. 191-197 ◽  
Author(s):  
K.-M. Wang
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Soluble Fraction ◽  
The Other ◽  
Acid Phosphatases ◽  
Peak Activity ◽  
Ph Optimum ◽  
Triton X ◽  
Soluble Fractions

1. The development, localization and heterogeneity of acid phosphatase and a Zn2+-activated acid phosphatase in cellular fractions of developing chick liver were studied. 2. Acid phosphatase is distributed abundantly in the particulate and soluble fractions. The soluble fraction is rich in Zn2+-activated acid phosphatase, which attains its peak activity at about 15 days of incubation. 3. The particulate acid phosphatase activity is inhibited by fluoride but not by sodium l(+)-tartrate or cysteine. On the other hand, the soluble Zn2+-activated acid phosphatase activity is inhibited by sodium l(+)-tartrate and cysteine but not by fluoride. 4. The pH optimum of these two enzymes is similar at about 5·6. 5. The soluble Zn2+-activated acid phosphatase activity appears to be thermally stabilized by the treatment with Triton X-100 or bovine serum albumin.

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).

Acid phosphatase activity in the Indian apple snail,Pila globosa (Swainson), during aestivation and starvation stress

1979 ◽  
Vol 88 (5) ◽  
pp. 363-365 ◽  
Author(s):  
P Aruna ◽  
C Sreeramulu Chetty ◽  
R Chandramohan Naidu ◽  
K S Swami
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Apple Snail ◽  
Starvation Stress ◽  
Pila Globosa
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