Acid phosphatase activity of intact roots and phosphorus nutrition in plants. 2. Variations among wheat roots

1980 ◽  
Vol 31 (3) ◽  
pp. 441 ◽  
Author(s):  
KD McLachlan

Variation in phosphatase activity (E.C. 3.1.3.41) in some cultivated wheats and wild progenitors was examined and a comparison made. The limits likely to occur in wheat were estimated, and the usefulness of phosphatase activity as an indicator of plant potential for exploiting low phosphorus status situations was explored. Under the test conditions, within the cultivated wheats, the phosphatase activity varied in optical density from 4.6 to 9.3 per g fresh weight (P < 0.001), and selections among wheats on this basis could be made. Phosphorus uptake and total dry matter yield were negatively related to phosphatase activity (r = - 0.80 and - 0.82 respectively, each P < 0.00l), providing further supportive evidence of the proposition that plants with lower phosphatase activities may gain and use phosphorus more readily than plants with higher ones. The phosphatase activity of wild and cultivated progenitors of modern wheats ranged in optical density from 15.5 to 45.4 per g fresh weight. All the cultivated species had low phosphatase activities which, on the basis of the proposition, suggests that some unconscious selection for ability to use low fertility situations may have occurred with the domestication of wheat. On the other hand, there was no apparent grouping according to geographic origin of earlier cultivars used in Australia with respect to phosphatase activity to suggest any conscious selection for ability to grow well on low phosphorus status soils.

1982 ◽  
Vol 33 (1) ◽  
pp. 1 ◽  
Author(s):  
KD McLachlan ◽  
DGde Marco

Eight wheat cultivars, selected on the basis of their root phosphatase (E.C. 3.1.3.4.1) activities to provide a range of phosphorus garnering abilities, experienced difficulty in taking up phosphorus from a nutrient solution containing 1 �M phosphorus, a level frequently found in the soil solution. Under the experimental conditions, total phosphorus uptake by the plants was not affected by root weight, length or fineness, nor by early plant vigour as indicated by relative leaf expansion rates during the first 3 days. With this low phosphorus source, standard root phosphatase activity was not related to phosphorus uptake but was related to total phosphorus content of the plants (r = -0.736; P < 0.01). When root phosphatase activity and total phosphorus content were determined on the same plants, the correlation was improved (r = -0.914; P < 0.001), which suggests that root phosphatase activity is a good indicator of the present phosphorus status of a plant. This suggestion was tested further by determining leaf and root phosphatase on wheat plants which were responding in yield and in phosphorus uptake to four levels of phosphorus supply. In actively growing plants, leaf phosphatase (E.C. 3.1.3.4.1) activity was better related to total phosphorus uptake (r = -0.963; P < 0.001) than was root phosphatase activity. At a second stage, where yields continued to increase but there was little change in the phosphorus content of the plant other than in its redistribution between component parts, root phosphatase was better related to total phosphorus uptake (r = -0.910; P < 0.001). Nevertheless leaf phosphatase activity was still significantly related to total phosphorus uptake (r = -0.853; P < 0.001), and could prove to be a useful measure of the phosphorus status of the growing plant. In all cases total phosphorus content and total yield were positively related (r = +0.94; P < 0.001).


Genetika ◽  
2005 ◽  
Vol 37 (2) ◽  
pp. 165-171 ◽  
Author(s):  
Vladislava Galovic ◽  
Zorana Kotaranin ◽  
Srbislav Dencic

Analyzed in this paper were the in vitro effects of drought stress in 13 genotypes of winter wheat, one genotype of spring wheat, and three Triticale genotypes of different geographic origin. Callus tissue was induced from immature zygotic embryos (10-15 days after pollination) on a modified MS nutrient medium. After two weeks, callus tissue was transplanted onto the same medium enriched with 5% high-molecular polyethylene glycol (PEG 6000), which was used as the stress agent to produce the effect of drought chemically. A control group of calluses was grown on an identical medium but without PEG. After four weeks of growing calluses on these mediums, we assessed callus mass survival ability of the genotypes before the transplantation as well as percentage reduction of callus fresh weight after the transplantation onto the nutrient medium with 5% PEG. Statistically significant differences were found among the genotypes in their response to the induced stress. The best survival ability before the transplantation was found in the genotype Mexicol20 (83%), while the lowest was recorded in Slavija (11.3%). Culture growing under stress conditions significantly reduced callus fresh weight in all of the genotypes. The lowest decrease of the callus mass relative to control was recorded in Rozofskaja (14.4%) and the highest in Miranovska (58.4%), indicating the genotypes' tolerance levels towards drought stress.


1995 ◽  
Vol 310 (1) ◽  
pp. 221-224 ◽  
Author(s):  
J F St-Denis ◽  
B Annabi ◽  
H Khoury ◽  
G van de Werve

The effect of histone II-A on glucose-6-phosphatase and mannose-6-phosphatase activities was investigated in relation to microsomal membrane permeability. It was found that glucose-6-phosphatase activity in histone II-A-pretreated liver microsomes was stimulated to the same extent as in detergent-permeabilized microsomes, and that the substrate specificity of the enzyme for glucose 6-phosphate was lost in histone II-A-pretreated microsomes, as [U-14C]glucose-6-phosphate hydrolysis was inhibited by mannose 6-phosphate and [U-14C]mannose 6-phosphate hydrolysis was increased. The accumulation of [U-14C]glucose from [U-14C]glucose 6-phosphate into untreated microsomes was completely abolished in detergent-treated vesicles, but was increased in histone II-A-treated microsomes, accounting for the increased glucose-6-phosphatase activity, and demonstrating that the microsomal membrane was still intact. The stimulation of glucose-6-phosphatase and mannose-6-phosphatase activities by histone II-A was found to be reversed by EGTA. It is concluded that the effects of histone II-A on glucose-6-phosphatase and mannose-6-phosphatase are not caused by the permeabilization of the microsomal membrane. The measurement of mannose-6-phosphatase latency to evaluate the intactness of the vesicles is therefore inappropriate.


1959 ◽  
Vol 39 (1) ◽  
pp. 98-107 ◽  
Author(s):  
E. Reinbergs ◽  
L. H. Shebeski

The differences in fertility of four colchicine-induced autotetraploid barley varieties (Brant, Montcalm, O.A.C. 21 and York) were determined and compared in four successive generations following the induction of tetraploidy. Despite a wide fertility range within each autotetraploid, the varieties tested varied considerably in their mean per cent fertility. Within each variety the mean per cent fertility remained relatively constant from generation to generation. The Montcalm tetraploid had the lowest mean fertility, fluctuating from generation to generation within a range of 6.0 to 10.1 per cent. The O.A.C. 21 tetraploid had the highest mean fertility, fluctuating within a range of 40.0 to 51.3 per cent.Significant differences in fertility of the four autotetraploid varieties were interpreted as indicating that seed-setting ability may be genetically controlled and, therefore, hybridization and subsequent selection could be a promising method for increasing fertility.Continuous selection for either high or low fertility from the C1 to C4 generation did not change the mean per cent fertility level in the O.A.C. 21 tetraploid.


2019 ◽  
Vol 11 (9) ◽  
pp. 2584 ◽  
Author(s):  
Hafiz Ahmed ◽  
Muhammad Sajjad ◽  
Mingju Li ◽  
Muhammad Azmat ◽  
Muhammad Rizwan ◽  
...  

Diminishing water resources as a result of excessive use of water for irrigation and climate change posture a severe global threat to food security. Herein, an experiment was conducted to determine the selection criteria for drought-tolerant bread wheat genotypes at the seedling stage using morphological and photosynthetic pigmentation-related traits. A panel of 105 wheat landraces, historical Pakistani varieties, and advance breeding lines were evaluated under normal and drought stress using factorial completely randomized design. The root length, fresh weight, dry weight, cell membrane thermo-stability, and chlorophyll b were positively correlated among themselves under both normal and stress conditions. Hence, selection of any one of these traits enhances the performance of other traits. The shoot length was non-significant and negatively associated with all other studied characters except relative water content. The results suggested that selection for shoot length could not improve genetic gain for drought tolerance. Out of 10 principal components (PCs), the first three PCs were showed significant genetic variation under both conditions. The first three PCs showed 74.6% and 76% cumulative genetic variation under normal and drought conditions, respectively. Based on PCA, 10 drought-tolerant and five drought-susceptible genotypes were identified. Overall results suggested that selection for root length, fresh weight, dry weight, cell membrane thermo-stability, and chlorophyll b at the seedling stage would improve genetic gain for drought tolerance. The outperforming genotypes under drought stress conditions can be useful in future wheat breeding programs, and early selection for the traits recommended in this study will be effective for developing high-yielding and drought-tolerant wheat varieties.


1972 ◽  
Vol 18 (8) ◽  
pp. 841-844 ◽  
Author(s):  
Diane L Fabiny-Byrd ◽  
Gerhard Ertingshausen

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.


1977 ◽  
Vol 162 (2) ◽  
pp. 423-433 ◽  
Author(s):  
J F Antoniw ◽  
H G Nimmo ◽  
S J Yeaman ◽  
P Cowen

Muscle extracts were subjected to fractionation with ethanol, chromatography on DEAE-cellulose, precipitation with (NH4)2SO4 and gel filtration on Sephadex G-200. These fractions were assayed for protein phosphatase activities by using the following seven phosphoprotein substrates: phosphorylase a, glycogen synthase b1, glycogen synthase b2, phosphorylase kinase (phosphorylated in either the alpha-subunit or the beta-subunit), histone H1 and histone H2B. Three protein phosphatases with distinctive specificities were resolved by the final gel-filtration step and were termed I, II and III. Protein phosphatase-I, apparent mol.wt. 300000, was an active histone phosphatase, but it accounted for only 10-15% of the glycogen synthase phosphatase-1 and glycogen synthase phosphatase-2 activities and 2-3% of the phosphorylase kinase phosphatase and phosphorylase phosphatase activity recovered from the Sephadex G-200 column. Protein phosphatase-II, apparent mol.wt. 170000, possessed histone phosphatase activity similar to that of protein phosphatase-I. It possessed more than 95% of the activity towards the alpha-subunit of phosphorylase kinase that was recovered from Sephadex G-200. It accounted for 10-15% of the glycogen synthase phosphatase-1 and glycogen synthase phosphatase-2 activity, but less than 5% of the activity against the beta-subunit of phosphorylase kinase and 1-2% of the phosphorylase phosphatase activity recovered from Sephadex G-200. Protein phosphatase-III was the most active histone phosphatase. It possessed 95% of the phosphorylase phosphatase and beta-phosphorylase kinase phosphatase activities, and 75% of the glycogen synthase phosphatase-1 and glycogen synthase phosphatase-2 activities recovered from Sephadex G-200. It accounted for less than 5% of the alpha-phosphorylase kinase phosphatase activity. Protein phosphatase-III was sometimes eluted from Sephadex-G-200 as a species of apparent mol.wt. 75000(termed IIIA), sometimes as a species of mol.wt. 46000(termed IIIB) and sometimes as a mixture of both components. The substrate specificities of protein phosphatases-IIA and -IIB were identical. These findings, taken with the observation that phosphorylase phosphatase, beta-phosphorylase kinase phosphatase, glycogen synthase phosphatase-1 and glycogen synthase phosphatase-2 activities co-purified up to the Sephadex G-200 step, suggest that a single protein phosphatase (protein phosphatase-III) catalyses each of the dephosphorylation reactions that inhibit glycogenolysis or stimulate glycogen synthesis. This contention is further supported by results presented in the following paper [Cohen, P., Nimmo, G.A. & Antoniw, J.F. (1977) Biochem. J. 1628 435-444] which describes a heat-stable protein that is a specific inhibitor of protein phosphatase-III.


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