Comparative studies of activity and properties of ferredoxin–NADP+ reductase during cold hardening of wheat

1976 ◽  
Vol 54 (16) ◽  
pp. 1896-1902 ◽  
Author(s):  
Joseph Riov ◽  
Gregory N. Brown
Keyword(s):  
Activation Energy ◽  
Spring Wheat ◽  
Comparative Studies ◽  
Low Temperatures ◽  
Specific Activity ◽  
Cold Hardening ◽  
Heat Inactivation ◽  
Enzyme Molecule ◽  
Enzyme Specific Activity ◽  
Michaelis Constants

Activity and properties of chloroplast ferredoxin–NADP− reductase (EC 1.6.7.1) were studied during cold hardening of two varieties of wheat (Triticum aestivnm), hardy Kharkov (winter wheat) and much less hardy Rescue (spring wheat), to determine whether adaptation to low temperatures involves changes in the activity and properties of this enzyme. Specific activity of ferredoxin–NADP− reductase increased during hardening of both varieties, but the increase was much greater in the more hardy variety, Kharkov 22 MC. No changes were found in the Michaelis constants for NADPH and 2,6-dichlorophenol indophenol, activation energy values, inhibition constants for p-chloromercuriphenylsulfonate, and sensitivity toward cold and heat inactivation of the enzyme from control and cold-hardened seedlings of both varieties. The data suggest that there is a preferential synthesis of ferredoxin–NADP− reductase during hardening of wheat, but the enzyme molecule remains unchanged.

Purification and Properties of Thymidylate Synthetase from Pig Thymus

1972 ◽  
Vol 50 (4) ◽  
pp. 352-362 ◽  
Author(s):  
V. S. Gupta ◽  
J. B. Meldrum
Keyword(s):  
Catalytic Activity ◽  
Sulfonic Acid ◽  
Specific Activity ◽  
Gel Filtration ◽  
Thymidylate Synthetase ◽  
Heat Inactivation ◽  
Synthetase Activity ◽  
Purification And Properties ◽  
Michaelis Constants ◽  
Sulfhydryl Compounds

Thymidylate synthetase of pig thymus has been separated into two principal forms (designated I and II, based on their order of elution) by chromatography on CM-Sephadex. By the use of (NH4)2SO4 the synthetase activity was separated into two fractions, and these were further purified by gel filtration using Sephadex G-100 and chromatography on CM-Sephadex. The highest specific activity obtained for I and II was 10.4 and 16.3 μmol of thymidine-5′-phosphate per hour per milligram of protein at 25° and pH 7.3 which represents a purification of 1680- and 2630-fold, respectively. Electrophoretically, I and II appear to be 70–80% pure. The Michaelis constants of 7.4 × 10−6 M, 1.7 × 10−5 M, and 1.8 × 10−4 M for II with respect to deoxyuridine-5′-phosphate, 5,10-methlenetetrahydrofolate, and uridine-5′-phosphate, respectively, have been determined. A double pH optima in the range of 6.6–6.8 and 7.2–7.4 in 2-N-morpholinoethane sulfonic acid buffer was exhibited by both forms. Forms I and II showed maximal catalytic activity only in the presence of sulfhydryl compounds (60 mM) and also had the ability to methylate uridine-5′-phosphate, although at a slower rate (ca. 28% and 13%, respectively) compared with the rate of methylation of deoxyuridine-5′-phosphate. Both deoxyuridine-5′-phosphate and tetrahydrofolate (to a lesser extent) afforded protection to II against heat inactivation.

Chloroplastic proteins of wheat and rye grown at warm and cold-hardening temperatures

1976 ◽  
Vol 54 (10) ◽  
pp. 848-853 ◽  
Author(s):  
Norman P. A. Huner ◽  
Fergus D. H. Macdowall
Keyword(s):  
Spring Wheat ◽  
Low Temperatures ◽  
Plant Material ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Cold Hardening ◽  
Fraction I Protein ◽  
Fraction I ◽  
Two Peaks ◽  
New Protein

Soluble proteins and membrane polypeptides were separated from chloroplasts isolated intact from a cultivar each of spring wheat, winter wheat, and more freeze-resistant rye, and changes in them associated with cold hardening were detected by means of polyacrylamide gel electrophoresis. No drastic changes in chloroplast membrane polypeptides occurred during growth at low temperatures in the three cultivars. However, subtle changes were evident in the soluble chloroplast protein fraction. In this fraction at least one varietal difference was discernable, yet all cultivars produced a new protein band of lowest mobility during growth at low temperatures. After the preparations were fractionated by Sephadex G-50 all unhardened plant material displayed two peaks in the region of the fraction I protein band, whereas all cold-hardened material displayed one peak. A different band of soluble protein was present only after cold hardening in Kharkov wheat and Puma rye, and was not present in extracts from the cold-grown spring wheat.

SOLUBLE SUGAR CHANGES OCCURRING DURING COLD HARDENING OF SPRING WHEAT, FALL RYE AND ALFALFA

1983 ◽  
Vol 63 (2) ◽  
pp. 415-420 ◽  
Author(s):  
D. G. GREEN
Keyword(s):  
Spring Wheat ◽  
Soluble Sugar ◽  
Soluble Sugars ◽  
Dry Weight ◽  
Weight Basis ◽  
Cold Hardening ◽  
Spring Type

Alfa, a relatively nonhardy alfalfa cultivar continued to accumulate, on a dry weight basis, fructose, α- and β-D-glucose, sucrose and maltose during the latter stages of cold hardening. Rambler, a hardier alfalfa cultivar conversely showed a decrease for these soluble sugars with hardening. Frontier rye, a very hardy winter habit cereal showed decreases in these soluble sugars plus melibiose during the same hardening period. These results support the hypothesis that hardy cereals and alfalfa undergo a decrease in soluble sugars with hardening, while less hardy cereals and alfalfa continue to increase in content of soluble sugars. Manitou wheat appeared not to fit this hypothesis and showed the decreased soluble sugars usually associated with hardy cultivars. Although Manitou is a spring type wheat, one of its parents, Thatcher, does contain gene(s) for the winter habit.Key words: Sugar, cold hardening, wheat, rye, alfalfa

Multiple Forms of Phosphoglyceromutase from Chicken Breast Muscle

1972 ◽  
Vol 50 (10) ◽  
pp. 1132-1142 ◽  
Author(s):  
Eric James ◽  
R. O. Hurst ◽  
T. G. Flynn
Keyword(s):  
Specific Activity ◽  
Gel Filtration ◽  
Diffusion Constant ◽  
Sedimentation Coefficient ◽  
Breast Muscle ◽  
Heat Inactivation ◽  
Chicken Breast ◽  
Multiple Forms ◽  
Active Components ◽  
Net Charges

Phosphoglyceromutase (2,3-diphospho-D-glycerate: 2-phospho-D-glycerate phosphotransferase, EC 2.7.5.3) has been purified from both frozen and fresh chicken breast muscle. During purification it was found that substrate, 3-phospho-D-glycerate stabilized the enzyme against heat inactivation to almost the same extent as did the cofactor 2,3-diphospho-D-glycerate.Phosphoglyceromutase prepared from frozen chicken breast muscle separated into three peaks of activity (I, II, and III) following chromatography on DEAE-Sephadex in 0.05 μ phosphate buffer, pH 8.0, using a 0.0–0.4 M NaCl gradient. Each peak of activity was shown by polyacrylamide disc gel electrophoresis at pH 9.3 to contain two enzymically active components (isoenzymes Ia Ib, IIa IIb, and IIIa IIIb). Isoenzymes in the same peak had the same specific activity. Phosphoglyceromutase prepared from fresh chicken breast muscle yielded only one peak of activity following chromatography on DEAE-Sephadex. This peak contained two enzymically active components corresponding to isoenzymes Ia and Ib. Additional peaks of activity were not produced when phosphoglyceromutase from fresh muscle was subjected to freezing and thawing.Isoenzyme Ia and mixtures of Ia and Ib, IIa and IIb, and IIIa and IIIb were homogeneous in the ultra-centrifuge sedimenting as single peaks. The sedimentation coefficient obtained for isoenzyme Ia and for Ia and Ib combined was 4.15 S, the diffusion constant 6.62 × 10−7 cm2/s, and the molecular weight calculated from both gel filtration and sedimentation data was of the order of 59 000. These results were confirmed by charge isomer studies which also showed that the isoenzymes of phosphoglyceromutase from frozen chicken breast muscle were proteins of the same size but different net charges.

Effect of light on the gene expression and hormonal status of winter and spring wheat plants during cold hardening

2012 ◽  
Vol 145 (2) ◽  
pp. 296-314 ◽  
Author(s):  
Imre Majláth ◽  
Gabriella Szalai ◽  
Vilmos Soós ◽  
Endre Sebestyén ◽  
Ervin Balázs ◽  
...  
Keyword(s):  
Gene Expression ◽  
Spring Wheat ◽  
Cold Hardening ◽  
Hormonal Status ◽  
Effect Of Light

scholarly journals Thermal dependence of the antioxidant enzymes superoxide dismutase, catalase, and peroxidase in foliage of Iris pumila L.

2009 ◽  
Vol 61 (3) ◽  
pp. 441-446 ◽  
Author(s):  
Ana Vuleta ◽  
Branka Tucic
Keyword(s):  
Activation Energy ◽  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Temperature Increase ◽  
Specific Activity ◽  
Thermal Dependence ◽  
Full Sunlight ◽  
Iris Pumila ◽  
Temperature Optima

Thermal dependence of the enzymes SOD, CAT, and POD was investigated in leaves of Iris pumila plants inhabiting two contrasting light environments, a sun-exposed dune site and a woodland understory. At the same assay temperature, both the specific activity and the activation energy of SOD and CAT were higher in plants inhabiting vegetation shade than in those experiencing full sunlight. Conversely, the temperature optima for the two enzymes did not differ between alternative radiation environments. The specific activity of POD increased with temperature increase, and was always greater in plants growing under full sunlight than in those from vegetation shade. The activation energy of POD was higher than that of SOD or CAT, being lower in sun-than in shade-exposed plants.

scholarly journals Improvement in Carbonization Efficiency of Cellulosic Fibres Using Silylated Acetylene and Alkoxysilanes

Fibers ◽  
2019 ◽  
Vol 7 (10) ◽  
pp. 84
Author(s):  
Maria Mironova ◽  
Igor Makarov ◽  
Lyudmila Golova ◽  
Markel Vinogradov ◽  
Georgy Shandryuk ◽  
...  
Keyword(s):  
Activation Energy ◽  
Thermal Decomposition ◽  
Thermal Behavior ◽  
Comparative Studies ◽  
Decomposition Reaction ◽  
Activation Energies ◽  
Composite Fibers ◽  
Carbon Yield ◽  
Pyrolysis Reaction ◽  
Cellulosic Fibres

Comparative studies of the structure and thermal behavior of cellulose and composite precursors with additives of silyl-substituted acetylene and alkoxysilanes were carried out. It is shown that the introduction of silicon-containing additives into the cellulose matrix influenced the thermal behavior of the composite fibers and the carbon yield after carbonization. Comparison of the activation energies of the thermal decomposition reaction renders it possible to determine the type of additive and its concentration, which reduces the energy necessary for pyrolysis. It is shown that the C/O ratio in the additive and the presence of the Si–C bond affected the activation energy and the temperature of the beginning and the end of the pyrolysis reaction.

Oxygen diffusion in amorphous and partially crystalline gallium oxide

2019 ◽  
Vol 21 (8) ◽  
pp. 4268-4275 ◽  
Author(s):  
Alexandra von der Heiden ◽  
Manuel Bornhöfft ◽  
Joachim Mayer ◽  
Manfred Martin
Keyword(s):  
Activation Energy ◽  
Diffusion Coefficients ◽  
Low Temperatures ◽  
Oxygen Diffusion ◽  
Gallium Oxide ◽  
Tracer Diffusion ◽  
Tof Sims ◽  
Tracer Diffusion Coefficients ◽  
Oxygen Tracer

We established a TTT diagram of crystallisation of gallium oxide. Determination of oxygen tracer diffusion coefficients by IEDP/ToF-SIMS allowed us to access the activation energy for amorphous GaO1.5 at low temperatures.

Zymographic approach to determine the intrinsic enzyme specific activity of diamine oxidase in presence of interfering enzymes

2017 ◽  
Vol 975 ◽  
pp. 78-85 ◽  
Author(s):  
Samaneh Ahmadifar ◽  
Tien Canh Le ◽  
Lucia Marcocci ◽  
Paola Pietrangeli ◽  
Mircea Alexandru Mateescu
Keyword(s):  
Diamine Oxidase ◽  
Specific Activity ◽  
Enzyme Specific Activity

THE THERMAL DECOMPOSITION OF HYDROGEN PEROXIDE VAPOUR. II.

1947 ◽  
Vol 25b (2) ◽  
pp. 135-150 ◽  
Author(s):  
Paul A. Giguère
Keyword(s):  
Activation Energy ◽  
Hydrogen Peroxide ◽  
Thermal Decomposition ◽  
Low Temperatures ◽  
Hydrocyanic Acid ◽  
Quartz Surface ◽  
First Order ◽  
Acid Washing ◽  
Reaction Vessels ◽  
Low Pressures

The decomposition of hydrogen peroxide vapour has been investigated at low pressures (5 to 6 mm.) in the temperature range 50° to 420 °C., for the purpose of determining the effect of the nature and treatment of the active surfaces. The reaction was followed in an all-glass apparatus and, except in one case, with one-litre round flasks as reaction vessels. Soft glass, Pyrex, quartz, and metallized surfaces variously treated were used. In most cases the decomposition was found to be mainly of the first order but the rates varied markedly from one vessel to another, even with vessels made of the same type of glass. On a quartz surface the decomposition was preceded by an induction period at low temperatures. Fusing the glass vessels slowed the reaction considerably and increased its apparent activation energy; this effect was destroyed by acid washing. Attempts to poison the surface with hydrocyanic acid gave no noticeable result. The marked importance of surface effects at all temperatures is considered as an indication that the reaction was predominantly heterogeneous under the prevailing conditions. Values ranging from 8 to 20 kcal. were found for the apparent energy of activation. It is concluded that the decomposition of hydrogen peroxide vapour is not very specific as far as the nature of the catalyst is concerned.

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