scholarly journals THYMIDINE DEGRADATION PRODUCTS IN PLANT TISSUES LABELED WITH TRITIATED THYMIDINE

1963 ◽  
Vol 17 (1) ◽  
pp. 59-66 ◽  
Author(s):  
S. T. Takats ◽  
R. M. S. Smellie
Keyword(s):  
Acetic Acid ◽  
Metabolic Pathways ◽  
Time Course ◽  
Degradation Products ◽  
Tritiated Thymidine ◽  
Lilium Longiflorum ◽  
Plant Tissues ◽  
Root Tips ◽  
Radioactivity Analysis ◽  
Ethanol Acetic Acid

A study of the metabolic pathways of H3-thymidine utilization in buds of Lilium longiflorum and root tips of Vicia faba was undertaken in order to obtain information that might explain the binding of H3 from H3-thymidine in the cytoplasm of these plants. H3-thymidine was administered for various periods of time, the tissues were fixed and processed in the manner routinely used in preparation for sectioning and autoradiography, and the radioactivity removed in this way from the tissues was determined. It was found that the ethanol/acetic acid fixative contained the major portion of the radioactivity. Analysis of this extract by paper chromatography showed that the radioactivity was distributed among various degradation products of thymidine, principally ß-ureidoisobutyric acid and ß-aminoisobutyric acid. Time course experiments with Vicia showed that these degradation products rapidly appeared in the tissue during incubation with H3-thymidine, while H3-thymine appeared in the incubation medium. Preliminary studies indicated that Vicia root tips incubated with H3-dihydrothymine for 24 hours would bind a small amount of H3 non-specifically in the cells. It seems unlikely that utilization of degradation products of H3-thymidine is sufficient to explain labeling which is concentrated in the cytoplasm.

Localization of acid phosphatases in root cap of rice plant

1991 ◽  
Vol 49 ◽  
pp. 224-225
Author(s):  
Y. R. Chen ◽  
Y. F. Huang ◽  
W. S. Chen
Keyword(s):  
Rice Plant ◽  
Developmental Stages ◽  
Uranyl Acetate ◽  
Root Cap ◽  
Plant Tissues ◽  
Acid Phosphatases ◽  
Root Tips ◽  
Buffer Solution ◽  
Cacodylate Buffer ◽  
Ethanol Series

Acid phosphatases are widely distributed in different tisssues of various plants. Studies on subcellular localization of acid phosphatases show they might be present in cell wall, plasma lemma, mitochondria, plastid, vacuole and nucleus. However, their localization in rice cell varies with developmental stages of cells and plant tissues. In present study, acid phosphatases occurring in root cap are examined.Sliced root tips of ten-day-old rice(Oryza sativa) seedlings were fixed in 0.1M cacodylate buffer containing 2.5% glutaraldehyde for 2h, washed overnight in same buffer solution, incubated in Gomori's solution at 37° C for 90min, post-fixed in OsO4, dehydrated in ethanol series and finally embeded in Spurr's resin. Sections were doubly stained with uranyl acetate and lead citrate, and observed under Hitachi H-600 at 75 KV.

Comparison of High Purity Factor IX Concentrates and a Prothrombin Complex Concentrate in a Canine Model of Thrombogenicity

1991 ◽  
Vol 66 (05) ◽  
pp. 609-613 ◽  
Author(s):  
I R MacGregor ◽  
J M Ferguson ◽  
L F McLaughlin ◽  
T Burnouf ◽  
C V Prowse
Keyword(s):  
High Purity ◽  
Time Course ◽  
Prothrombin Complex Concentrate ◽  
Degradation Products ◽  
Canine Model ◽  
Factor Ix ◽  
In Vitro Tests ◽  
Albumin Infusion

SummaryA non-stasis canine model of thrombogenicity has been used to evaluate batches of high purity factor IX concentrates from 4 manufacturers and a conventional prothrombin complex concentrate (PCC). Platelets, activated partial thromboplastin time (APTT), fibrinogen, fibrin(ogen) degradation products and fibrinopeptide A (FPA) were monitored before and after infusion of concentrate. Changes in FPA were found to be the most sensitive and reproducible indicator of thrombogenicity after infusion of batches of the PCC at doses of between 60 and 180 IU/kg, with a dose related delayed increase in FPA occurring. Total FPA generated after 100-120 IU/kg of 3 batches of PCC over the 3 h time course was 9-12 times that generated after albumin infusion. In contrast the amounts of FPA generated after 200 IU/kg of the 4 high purity factor IX products were in all cases similar to albumin infusion. It was noted that some batches of high purity concentrates had short NAPTTs indicating that current in vitro tests for potential thrombogenicity may be misleading in predicting the effects of these concentrates in vivo.

Aminocyclopyrachlor Absorption, Translocation and Metabolism in Field Bindweed (Convolvulus arvensis)

Weed Science ◽  
2013 ◽  
Vol 61 (1) ◽  
pp. 63-67 ◽  
Author(s):  
R. Bradley Lindenmayer ◽  
Scott J. Nissen ◽  
Philip P. Westra ◽  
Dale L. Shaner ◽  
Galen Brunk
Keyword(s):  
Plant Tissue ◽  
Time Course ◽  
Plant Tissues ◽  
Laboratory Studies ◽  
Weed Species ◽  
Convolvulus Arvensis ◽  
Single Leaf ◽  
Field Bindweed ◽  
Treated Leaf ◽  
Aboveground Tissue

Field bindweed is extremely susceptible to aminocyclopyrachlor compared to other weed species. Laboratory studies were conducted to determine if absorption, translocation, and metabolism of aminocyclopyrachlor in field bindweed differs from other, less susceptible species. Field bindweed plants were treated with 3.3 kBq14C-aminocyclopyrachlor by spotting a single leaf mid-way up the stem with 10 µl of herbicide solution. Plants were then harvested at set intervals over 192 h after treatment (HAT). Aminocyclopyrachlor absorption reached a maximum of 48.3% of the applied radioactivity by 48 HAT. A translocation pattern of herbicide movement from the treated leaf into other plant tissues emerged, revealing a nearly equal aminocyclopyrachlor distribution between the treated leaf, aboveground tissue, and belowground tissue of 13, 14, and 14% of the applied radioactivity by 192 HAT. Over the time-course, no soluble aminocyclopyrachlor metabolites were observed, but there was an increase in radioactivity recovered bound in the nonsoluble fraction. These results suggest that aminocyclopyrachlor has greater translocation to belowground plant tissue in field bindweed compared with results from other studies with other herbicides and other weed species, which could explain the increased level of control observed in the field. The lack of soluble metabolites also suggests that very little metabolism occurred over the 192 h time course.

scholarly journals Fabrication of TiO2/Carbon Photocatalyst using Submerged DC Arc Discharged in Ethanol/Acetic Acid Medium

2017 ◽  
Vol 202 ◽  
pp. 012058 ◽  
Author(s):  
T E Saraswati ◽  
A O Nandika ◽  
I F Andhika ◽  
Patiha ◽  
C Purnawan ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Acid Medium ◽  
Acetic Acid Medium ◽  
Ethanol Acetic Acid ◽  
Dc Arc

Characteristics of Piperine Solubility in Multiple Solvent

2011 ◽  
Vol 236-238 ◽  
pp. 2495-2498 ◽  
Author(s):  
Xue Song Huang ◽  
Xian Zhe Lin ◽  
Mo Ting Guo ◽  
Ya Zou
Keyword(s):  
Experimental Data ◽  
High Performance Liquid Chromatography ◽  
Acetic Acid ◽  
High Performance ◽  
Authentic Sample ◽  
Allometric Model ◽  
Experiment Data ◽  
Reverse Phase ◽  
Ethanol Acetic Acid ◽  
Acetic Acid Water

The solution of piperine in multiple solvent including ethanol, acetic acid, water and HCl were investigated to extract more piperine from piper fruit. Piperine was determined by reverse phase high-performance liquid chromatography with Diamonsil column (C18,5 μm ,250 mm×4. 6 mm) at 343 nm. Experiment data were simulated by Allometric model and the formula is Z=0.9+ 4.54×10-10×x5.675+1.8029×y2.12848+2.37×10-10×x5.675×y2.12848(Z:sample solution,mol/mL,x: the percentage of ethanol’s volume, ml/100mL,y: the acetic acid in the authentic sample solution, g/100mL), the adj·R2=0.997, the comparative deviation less than 2%. These results are good in agreement with experimental data. It reveals that the model can meet the requirements of the selection and design in extracting piperine from piper fruit.

scholarly journals The Role of Arabinogalactan Type II Degradation in Plant-Microbe Interactions

2021 ◽  
Vol 12 ◽  
Author(s):  
Maria Guadalupe Villa-Rivera ◽  
Horacio Cano-Camacho ◽  
Everardo López-Romero ◽  
María Guadalupe Zavala-Páramo
Keyword(s):  
Cell Wall ◽  
Plant Defense ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Degradation Products ◽  
Hydrolytic Enzymes ◽  
Pathogenic Fungi ◽  
Plant Interactions ◽  
Root Tips ◽  
Microbe Interactions

Arabinogalactans (AGs) are structural polysaccharides of the plant cell wall. A small proportion of the AGs are associated with hemicellulose and pectin. Furthermore, AGs are associated with proteins forming the so-called arabinogalactan proteins (AGPs), which can be found in the plant cell wall or attached through a glycosylphosphatidylinositol (GPI) anchor to the plasma membrane. AGPs are a family of highly glycosylated proteins grouped with cell wall proteins rich in hydroxyproline. These glycoproteins have important and diverse functions in plants, such as growth, cellular differentiation, signaling, and microbe-plant interactions, and several reports suggest that carbohydrate components are crucial for AGP functions. In beneficial plant-microbe interactions, AGPs attract symbiotic species of fungi or bacteria, promote the development of infectious structures and the colonization of root tips, and furthermore, these interactions can activate plant defense mechanisms. On the other hand, plants secrete and accumulate AGPs at infection sites, creating cross-links with pectin. As part of the plant cell wall degradation machinery, beneficial and pathogenic fungi and bacteria can produce the enzymes necessary for the complete depolymerization of AGs including endo-β-(1,3), β-(1,4) and β-(1,6)-galactanases, β-(1,3/1,6) galactanases, α-L-arabinofuranosidases, β-L-arabinopyranosidases, and β-D-glucuronidases. These hydrolytic enzymes are secreted during plant-pathogen interactions and could have implications for the function of AGPs. It has been proposed that AGPs could prevent infection by pathogenic microorganisms because their degradation products generated by hydrolytic enzymes of pathogens function as damage-associated molecular patterns (DAMPs) eliciting the plant defense response. In this review, we describe the structure and function of AGs and AGPs as components of the plant cell wall. Additionally, we describe the set of enzymes secreted by microorganisms to degrade AGs from AGPs and its possible implication for plant-microbe interactions.

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