THE NATURE OF STARCH ACCUMULATION AT THE RUST INFECTION SITE IN LEAVES OF PINTO BEAN PLANTS

1961 ◽  
Vol 39 (7) ◽  
pp. 1595-1604 ◽  
Author(s):  
Dalton Wang
Keyword(s):  
De Novo ◽  
Host Tissue ◽  
Starch Accumulation ◽  
Infected Leaf ◽  
Infection Site ◽  
De Novo Synthesis ◽  
Rust Infection ◽  
Carbon 14 ◽  
Wheat Leaves ◽  
Green Island

The accumulation of radioactivity from carbon-14 dioxide assimilation at infection sites of Uromyces phaseoli was studied. The accumulated radioactivity was found to reside essentially in starch, which has been clearly demonstrated in this study to be the result of de novo synthesis from carbon-14 dioxide at the infection site and not due to an enhanced translocation of photosynthates from non-infected leaf areas and subsequent starch synthesis.It was also shown that U. phaseoli induced an increase in the chlorophyll content of the host tissue located at the periphery of the rust colony as it developed, and a concomitant increase in starch accumulation.Unlike the ‘green island' induced by powdery mildew in wheat leaves reported by Allen, the 'green island' induced by U. phaseoli in bean leaves is the result of pigment retention in the host tissue within the domain of influence of the parasite. The chlorophyll in the 'green island' was found to be photosynthetically active. Results from experiments of photosynthesis with 'green islands' provided the unequivocal evidence to support the idea of de novo synthesis of starch at the sites of rust infection.

A STUDY OF THE DISTRIBUTION OF CARBON-14 LABELLED COMPOUNDS IN STEM RUST INFECTED WHEAT LEAVES

1960 ◽  
Vol 38 (4) ◽  
pp. 635-642 ◽  
Author(s):  
Dalton Wang
Keyword(s):  
Stem Rust ◽  
Infected Leaf ◽  
Actual Concentration ◽  
X Ray ◽  
Carbon 14 ◽  
Tissue Sections ◽  
Quantitative Measurements ◽  
Specific Distribution ◽  
Two Factors ◽  
Wheat Leaves

Glucose-U-C14, glycine-2-C14, benzimidazole-2-C14, as well as C14O2, were fed to rusted leaves of Little Club wheat. Radioautographs of whole leaves gave similar results to those of previous investigators, indicating greater radioactivity in rust ed tissue sections. However, when quantitative measurements were made the results indicated that rusted tissue sections do not contain more radioactivity than the healthy tissue sections despite the apparent accumulation of labelled com pounds at infection sites indicated by radioautographs of the treated leaves. The apparent accumulation of radioactivity at the infection sites of rusted leaves may not, therefore, represent the actual concentration of the labelled compounds throughout the infected leaf. The phenomenon of radioactivity accumulation indicated by radioautographs may be attributed to two factors: (a) the geometric factor in respect to radioactive sources to the X-ray film and (b) the specific distribution in respect to the higher radioactivity in the rapidly growing regions of the fungus.

INCORPORATION OF CYTIDINE-H3 INTO THE PRIMARY LEAF OF WHEAT FOLLOWING INFECTION WITH PUCCINIA RECONDITA ROB. EX DESM.

1963 ◽  
Vol 41 (10) ◽  
pp. 1501-1508 ◽  
Author(s):  
J. Nielsen ◽  
R. Rohringer
Keyword(s):  
Host Cell ◽  
Ribonucleic Acid ◽  
Host Tissue ◽  
Host Cells ◽  
Puccinia Recondita ◽  
Infected Leaf ◽  
Cell Nuclei ◽  
Short Term ◽  
Wheat Leaves ◽  
Host Parasite

In short-term experiments, cytidine-H3 was fed to rusted and healthy areas of wheat leaves. The incorporated activity, presumably residing in ribonucleic acid, was detected by microautoradiographic methods. Most of the label was found to be incorporated in host cell nuclei. Little incorporation occurred in extranuclear structures of host cells, including chloroplasts. Very long autoradiographic exposure times failed to reveal any incorporation into the fungus.Host cells in infected leaf areas contained considerably less label in their nuclei and cytoplasm than those in cells further from the site of infection. This effect of the fungus extended over some distance into uninvaded host tissue, but not beyond 100 μ from the periphery of the mycelium. The decreased cytidine incorporation in the affected host tissue is not caused by possible changes in pool size of endogenous cytidine. The significance of these results for the host–parasite interaction is briefly discussed.

Characterization of Monocyte-Associated Factor V

1993 ◽  
Vol 70 (02) ◽  
pp. 273-280 ◽  
Author(s):  
Janos Kappelmayer ◽  
Satya P Kunapuli ◽  
Edward G Wyshock ◽  
Robert W Colman
Keyword(s):  
Monoclonal Antibody ◽  
Light Chain ◽  
Peripheral Blood ◽  
De Novo ◽  
Factor V ◽  
Blood Monocytes ◽  
De Novo Synthesis ◽  
Hep G2 ◽  
Hep G2 Cells ◽  
Peripheral Blood Monocytes

SummaryWe demonstrate that in addition to possessing binding sites for intact factor V (FV), unstimulated peripheral blood monocytes also express activated factor V (FVa) on their surfaces. FVa was identified on the monocyte surface by monoclonal antibody B38 recognizing FVa light chain and by human oligoclonal antibodies H1 (to FVa light chain) and H2 (to FVa heavy chain) using immunofluorescence microscopy and flow cytometry. On Western blots, partially cleaved FV could be identified as a 220 kDa band in lysates of monocytes. In addition to surface expression of FVa, monocytes also contain intracellular FV as detected only after permeabilization by Triton X-100 by monoclonal antibody B10 directed specifically to the Cl domain not present in FVa. We sought to determine whether the presence of FV in peripheral blood monocytes is a result of de novo synthesis.Using in situ hybridization, no FV mRNA could be detected in monocytes, while in parallel control studies, factor V mRNA was detectable in Hep G2 cells and CD18 mRNA in monocytes. In addition, using reverse transcriptase and the polymerase chain reaction, no FV mRNA was detected in mononuclear cells or in U937 cells, but mRNA for factor V was present in Hep G2 cells using the same techniques. These data suggest that FV is present in human monocytes, presumably acquired by binding of plasma FV, and that the presence of this critical coagulation factor is not due to de novo synthesis.

Platelets Stimulate Thromboplastin Synthesis in Human Endothelial Cells

1983 ◽  
Vol 49 (02) ◽  
pp. 069-072 ◽  
Author(s):  
U L H Johnsen ◽  
T Lyberg ◽  
K S Galdal ◽  
H Prydz
Keyword(s):  
Endothelial Cells ◽  
De Novo ◽  
Umbilical Vein ◽  
Time Dependent ◽  
De Novo Synthesis ◽  
Human Endothelial Cells ◽  
Tumor Promotor ◽  
Coagulation Assay ◽  
Platelet Aggregates ◽  
Umbilical Vein Endothelial Cells

SummaryHuman umbilical vein endothelial cells in culture synthesize thromboplastin upon stimulation with phytohaemagglutinin (PHA) or the tumor promotor 12-O-tetradecanoyl-phorbol-13-acetate (TPA). The thromboplastin activity is further strongly enhanced in a time dependent reaction by the presence of gel-filtered platelets or platelet aggregates. This effect was demonstrable at platelet concentrations lower than those normally found in plasma, it may thus be of pathophysiological relevance. The thromboplastin activity increased with increasing number of platelets added. Cycloheximide inhibited the increase, suggesting that de novo synthesis of the protein component of thromboplastin, apoprotein III, is necessary.When care was taken to remove monocytes no thromboplastin activity and no apoprotein HI antigen could be demonstrated in suspensions of gel-filtered platelets, platelets aggregated with thrombin or homogenized platelets when studied with a coagulation assay and an antibody neutralization technique.

DE NOVO SYNTHESIS OF STEROIDS BY THE TESTES OF THE HUMAN FOETUS AT MIDGESTATION

1971 ◽  
Vol 68 (1_Supplb) ◽  
pp. S135 ◽  
Author(s):  
R. S. Mathur ◽  
N. Wiqvist ◽  
E. Diczfalusy
Keyword(s):  
De Novo ◽  
De Novo Synthesis ◽  
Human Foetus

In vivo study of the biosynthesis of long-chain fatty acids using deuterated water

1995 ◽  
Vol 269 (2) ◽  
pp. E247-E252 ◽  
Author(s):  
H. O. Ajie ◽  
M. J. Connor ◽  
W. N. Lee ◽  
S. Bassilian ◽  
E. A. Bergner ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
De Novo ◽  
Chain Elongation ◽  
Deuterated Water ◽  
De Novo Synthesis ◽  
Isotopomer Distribution ◽  
Long Chain ◽  
Mass Isotopomer

To determine the contributions of preexisting fatty acid, de novo synthesis, and chain elongation in long-chain fatty acid (LCFA) synthesis, the synthesis of LCFAs, palmitate (16:0), stearate (18:0), arachidate (20:0), behenate (22:0), and lignocerate (24:0), in the epidermis, liver, and spinal cord was determined using deuterated water and mass isotopomer distribution analysis in hairless mice and Sprague-Dawley rats. Animals were given 4% deuterated water for 5 days or 8 wk in their drinking water. Blood was withdrawn at the end of these times for the determination of deuterium enrichment, and the animals were killed to isolate the various tissues for lipid extraction for the determination of the mass isotopomer distributions. The mass isotopomer distributions in LCFA were incompatible with synthesis from a single pool of primer. The synthesis of palmitate, stearate, arachidate, behenate, and lignocerate followed the expected biochemical pathways for the synthesis of LCFAs. On average, three deuterium atoms were incorporated for every addition of an acetyl unit. The isotopomer distribution resulting from chain elongation and de novo synthesis can be described by the linear combination of two binomial distributions. The proportions of preexisting, chain elongation, and de novo-synthesized fatty acids as a percentage of the total fatty acids were determined using multiple linear regression analysis. Fractional synthesis was found to vary, depending on the tissue type and the fatty acid, from 47 to 87%. A substantial fraction (24-40%) of the newly synthesized molecules was derived from chain elongation of unlabeled (recycled) palmitate.

scholarly journals An enzymatic activation of formaldehyde for nucleotide methylation

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Charles Bou-Nader ◽  
Frederick W. Stull ◽  
Ludovic Pecqueur ◽  
Philippe Simon ◽  
Vincent Guérineau ◽  
...  
Keyword(s):  
Amino Acids ◽  
Thymidylate Synthase ◽  
Active Site ◽  
De Novo ◽  
Crystallographic Structure ◽  
De Novo Synthesis ◽  
Active Site Residues ◽  
Enzymatic Activation ◽  
Enzyme Cofactors ◽  
Unique Ability

AbstractFolate enzyme cofactors and their derivatives have the unique ability to provide a single carbon unit at different oxidation levels for the de novo synthesis of amino-acids, purines, or thymidylate, an essential DNA nucleotide. How these cofactors mediate methylene transfer is not fully settled yet, particularly with regard to how the methylene is transferred to the methylene acceptor. Here, we uncovered that the bacterial thymidylate synthase ThyX, which relies on both folate and flavin for activity, can also use a formaldehyde-shunt to directly synthesize thymidylate. Combining biochemical, spectroscopic and anaerobic crystallographic analyses, we showed that formaldehyde reacts with the reduced flavin coenzyme to form a carbinolamine intermediate used by ThyX for dUMP methylation. The crystallographic structure of this intermediate reveals how ThyX activates formaldehyde and uses it, with the assistance of active site residues, to methylate dUMP. Our results reveal that carbinolamine species promote methylene transfer and suggest that the use of a CH2O-shunt may be relevant in several other important folate-dependent reactions.

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