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.

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.

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

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 Weissellicin 110, a Newly Discovered Bacteriocin from Weissella cibaria 110, Isolated from Plaa-Som, a Fermented Fish Product from Thailand

2007 ◽  
Vol 73 (7) ◽  
pp. 2247-2250 ◽  
Author(s):  
Sirinat Srionnual ◽  
Fujitoshi Yanagida ◽  
Li-Hsiu Lin ◽  
Kuang-Nan Hsiao ◽  
Yi-sheng Chen
Keyword(s):  
Proteolytic Enzymes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Band ◽  
Proteinase K ◽  
Mass Spectrometry Analysis ◽  
Fermented Fish ◽  
Spectrometry Analysis ◽  
Weissella Cibaria ◽  
Fish Product

ABSTRACT Weissella cibaria 110, isolated from the Thai fermented fish product plaa-som, was found to produce a bacteriocin active against some gram-positive bacteria. Bacteriocin activity was not eliminated by exposure to high temperatures or catalase but was destroyed by exposure to the proteolytic enzymes proteinase K and trypsin. The bacteriocin from W. cibaria 110 was purified, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the purified bacteriocin contained one protein band that was approximately 2.5 kDa in size. Mass spectrometry analysis showed the mass of the peptide to be approximately 3,487.8 Da. N-terminal amino acid sequence analysis was performed, and 27 amino acids were identified. Because it has no similarity to other known bacteriocins, this bacteriocin was defined as a new bacteriocin and termed weissellicin 110.

scholarly journals Evaluation of SDS-Polyacrylamide gel electrophoresis and immunostrip technique for detection of Tobacco mosaic virus and Cucumber mosaic virus in IRAQ

2011 ◽  
Vol 5 (2) ◽  
pp. 85-94
Author(s):  
Rakib A. Al-Ani ◽  
Mustafa A. Adhab
Keyword(s):  
Tobacco Mosaic Virus ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Positive Reaction ◽  
Total Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Polyacrylamide Gel ◽  
Total Proteins ◽  
Winter Squash

his study was carried out to evaluate the efficiency of electrophoresis on SDS- poly acrylamide slap gel and immunostrip techniques for detection of Tobacco mosaic virus (TMV, genus Tobamovirus) and Cucumber mosaic virus (CMV, genus Cucumovirus, family Bromoviridae), compared with symptoms on diagnostic plants for the two viruses. The results obtained showed that the two methods were effective. The analysis of samples of purified CMV, total proteins from infected cucumber plants, and extracts from infected plants with or without chlorophyll, by electrophoresis on 10% polyacrylamide slap gel containing 0.1% SDS showed two bands of 24 and 26 kd in size, and absent in samples of total protein or extracts of healthy plants. These two proteins represent the coat protein (CP) of CMV. In addition, one 18 kd protein band appeared on SDS- polyacrylamide gel profile which represent the CP of TMV, when samples of purified virus, total protein of infected plants, and plant extracts with or without chlorophyll were analyzed. This band was absent in similar samples from healthy plants. The test of immunostrip specific for CMV showed positive reaction with extracts from melon, cucumber, winter squash, and zucchini infected plants. Similarly, a positive reaction with immunostrip specific for TMV appeared with extracts from tobacco, tomato infected with TMV. No reaction was obtained with healthy plants extract. These results were similar to those obtained from indicator plants for the two viruses.

scholarly journals Differential Localization of Fraction I Protein between Chloroplast Types

1976 ◽  
Vol 57 (5) ◽  
pp. 730-733 ◽  
Author(s):  
Steven C. Huber ◽  
Timothy C. Hall ◽  
Gerald E. Edwards
Keyword(s):  
Fraction I Protein ◽  
Differential Localization ◽  
Fraction I

Differences in the biochemical compositions and elicitor activity of extracellular components produced by three races of a fungal plant pathogen, Colletotrichum lindemuthianum

1980 ◽  
Vol 26 (12) ◽  
pp. 1473-1479 ◽  
Author(s):  
Aaanne J. Anderson
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Colletotrichum Lindemuthianum ◽  
Neutral Sugar ◽  
Sugar Composition ◽  
Fungal Plant Pathogen ◽  
Red Kidney Bean ◽  
Weakly Virulent ◽  
Protein Components ◽  
Highly Virulent

High molecular weight products from the α, β, and γ races of Colletotrichum lin-differed in their carbohydrate and protein compositions and in their abilities to elicit symptoms of a hypersensitive response in dark red kidney bean. The neutral sugar composition of the products varied in their proportions of rhamnose, mannose, galactose, and glucose. Polyacrylamide gel electrophoresis showed the protein components to be more numerous in the β race products than in the α or γ race products. Each protein band co-stained for carbohydrate. Highest elicitor activity was observed in the products from the α race, a race avirulent on dark red kidney. The products from the weakly virulent γ race were about 10-fold less active as elicitors than those of the α race. With the β race, a race highly virulent on dark red kidney, elicitor activity was 100-fold less than that of the α race.

Thrombin-Induced Surface Changes of Human Platelets in Plasma: Their Relation to Serotonin Release

1979 ◽  
Author(s):  
K. Subbarao ◽  
V.V. Kakkar
Keyword(s):  
Membrane Proteins ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Human Platelets ◽  
Serotonin Release ◽  
Glycoprotein I ◽  
Reversible Aggregation ◽  
Coomassie Blue ◽  
Labeling Pattern

Membrane proteins of both control and thrombin-treated platelets were labeled by NaB3H4, reduction of Schiff bases formed between pyridoxal 5′-phosphate and protein amino groups. Examination of the labeled polypeptides by SDS-polyacrylamide gel electrophoresis and fluorography disclosed a different labeling pattern for thrombin-treated platelets. The distributions of Coomassie blue-stained protein from treated and untreated cells were, by contrast, almost identical. Fluorographs of control platelets showed a single intensely labeled protein band (mol wt 90,000) whereas with cells exposed to thrombin (30-60 milliunits) about 10 protein bands with mol wts ranging from 43,000 to 200,000 were typically present. Among these were: thrombin-sensitive protein (mol wt 188,000), glycoprotein I (mol wt 150,000) and actin (mol wt 43,000). When serotonin release was prevented, either by reversing platelet aggregation with low amounts of ADP (0.1-0.3 μM) or by preincubating with 3',5'-ADP (20 μM), an inhibitor of both ADP- and thrombin-induced platelet function, the labeling patterns on fluorographs were similar to the control. These results indicate that blood platelets can undergo reversible aggregation without major changes in their surface topography, whereas thrombin-induced serotonin release appears related to structural alterations in platelet membrane proteins.

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