scholarly journals Proteomics research and related functional classification of liquid sclerotial exudates of Sclerotinia ginseng

PeerJ ◽  
2017 ◽  
Vol 5 ◽  
pp. e3979 ◽  
Author(s):  
Dan Wang ◽  
Jun Fan Fu ◽  
Ru Jun Zhou ◽  
Zi Bo Li ◽  
Yu Jiao Xie
Keyword(s):  
Life Cycle ◽  
Carbohydrate Metabolism ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Reduction Process ◽  
Protein Composition ◽  
Fungal Cell ◽  
Soil Pathogen ◽  
Oxidation Reduction ◽  
Fungal Life Cycle

Sclerotinia ginseng is a necrotrophic soil pathogen that mainly infects the root and basal stem of ginseng, causing serious commercial losses. Sclerotia, which are important in the fungal life cycle, are hard, asexual, resting structures that can survive in soil for several years. Generally, sclerotium development is accompanied by the exudation of droplets. Here, the yellowish droplets of S. ginseng were first examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the proteome was identified by a combination of different analytical platforms. A total of 59 proteins were identified and classified into six categories: carbohydrate metabolism (39%), oxidation-reduction process (12%), transport and catabolism (5%), amino acid metabolism (3%), other functions (18%), and unknown protein (23%), which exhibited considerable differences in protein composition compared with droplets of S. sclerotium. In the carbohydrate metabolism group, several proteins were associated with sclerotium development, particularly fungal cell wall formation. The pathogenicity and virulence of the identified proteins are also discussed in this report. The findings of this study may improve our understanding of the function of exudate droplets as well as the life cycle and pathogenesis of S. ginseng.

Changes in total and individual proteins during drying and ruminal fermentation of alfalfa

2005 ◽  
Vol 2005 ◽  
pp. 198-198
Author(s):  
A. A. Sadeghi ◽  
P. Shawrang ◽  
M. Moradi ◽  
A. Nikkhah
Keyword(s):  
Crude Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Plant Proteins ◽  
Ruminal Fermentation ◽  
Protein Nitrogen ◽  
Sds Page ◽  
Total Crude Protein ◽  
Hydrolysis Of

Proteolysis within plant cells occurs during wilting and drying. Changes in plant proteins during those periods usually are monitored by measurement of total crude protein and non protein nitrogen. Alternatively, changes in concentrations of individual proteins can be measured. Plants are composed of an array of different proteins. Electrophoresis can be used to separate these proteins and has been used to study effects of wilting and ensiling on proteins of some forages (Grum et al., 1991). Electrophoresis also has been used in the study of ruminal hydrolysis of oilseed meals proteins (Sadeghi et al., 2004). Most of the experiments designed to use electrophoresis to study protein metabolism in forages and ruminants have been qualitative. The main objective of this study was to determine whether sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and densitometry could be used to monitor quantitatively the changes in alfalfa protein composition during wilting, drying and ruminal exposure.

scholarly journals PROTEINS OF THE POSTSYNAPTIC DENSITY

1974 ◽  
Vol 63 (2) ◽  
pp. 456-465 ◽  
Author(s):  
G. Banker ◽  
L. Churchill ◽  
C. W. Cotman
Keyword(s):  
Molecular Weight ◽  
Plasma Membrane ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Synaptic Plasma Membrane ◽  
Brain Protein ◽  
Single Polypeptide ◽  
Structural Matrix ◽  
Polypeptide Band

An analysis was made of the protein composition of a fraction of postsynaptic densities (PSDs) prepared from rat brain. Protein makes up 90% of the material in the PSD fraction. Two major polypeptide fractions are present, based on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The major polypeptide fraction has a molecular weight of 53,000, makes up about 45% of the PSD protein, and comigrates on gels with a major polypeptide of the synaptic plasma membrane. The other polypeptide band has a molecular weight of 97,000, accounts for 17% of the PSD protein, and is not a prominent constituent of other fractions. Six other polypeptides of higher molecular weight (100,000–180,000) are consistently present in small amounts (3–9% each). The PSD fraction contains slightly greater amounts of polar amino acids and proline than the synaptic plasma membrane fraction, but no amino acid is usually prominent. The PSD apparently consists of a structural matrix formed primarily by a single polypeptide or class of polypeptides of 53,000 molecular weight. Small amounts of other specialized proteins are contained within this matrix.

Protein composition of Methanococcus thermolithotrophicus flagella

1992 ◽  
Vol 38 (11) ◽  
pp. 1162-1166 ◽  
Author(s):  
Alla S. Kostyukova ◽  
Georgi M. Gongadze ◽  
Anna Ya. Obraztsova ◽  
Konstantin S. Laurinavichus ◽  
Oleg V. Fedorov
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Key Words ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Complete Removal ◽  
Methanococcus Thermolithotrophicus ◽  
Molecular Weights ◽  
Dodecyl Sulfate

Sodium dodecyl sulfate – polyacrylamide gel electrophoresis of flagella from the thermophilic methanogen Methanococcus thermolithotrophicus indicated that they were composed of three major proteins, with molecular weights of 62 000,44 000, and 26 000, whereas all previously studied flagella of mesophilic methanogens consisted of two subunits. Proteins were isolated by preparative electrophoresis followed by complete removal of sodium dodecyl sulfate and their renaturation. It was shown that at least two of the proteins contain a thermostable domain whose complete denaturation proceeds only upon prolonged boiling in the presence of sodium dodecyl sulfate. Key words: flagellin, thermostability, archaebacteria, Methanococcus thermolithotrophicus.

scholarly journals Specific and azurophilic granules from rabbit polymorphonuclear leukocytes. I. Isolation and characterization of membrane and content subfractions.

1983 ◽  
Vol 96 (4) ◽  
pp. 1030-1039 ◽  
Author(s):  
W J Brown ◽  
W A Shannon ◽  
W J Snell
Keyword(s):  
Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Granule Protein ◽  
Isolation And Characterization ◽  
Cytoplasmic Face ◽  
Sds Page ◽  
Granule Membrane ◽  
Granule Membrane Proteins

The specific and azurophilic granules of rabbit polymorphonuclear heterophils (PMNs) have been isolated and fractionated into membrane and extractable subfractions. Analysis by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE) revealed several features of the protein composition of the two granules: (a) Whereas each type of granule had 40-60 proteins separable on one-dimensional gradient gels, few of the proteins were common to both granules. (b) The proteins of the extractable fractions (which comprised approximately 98% of the total granule protein) of each granule were distinct from the proteins of the membrane fractions (which comprised approximately 2% of the total granule protein). (c) The extractable proteins co-migrated with those collected from the medium of ionophore-treated, degranulating PMNs and therefore were defined as content proteins. These results were confirmed by radiolabeling studies. Lactoperoxidase-catalyzed iodination of intact granules did not label the content proteins but did label proteins that co-migrated with major granule membrane proteins. Moreover, disruption of the granules before iodination led to labeling of both content and membrane proteins. We conclude that the membranes of specific and azurophilic granules, which arise from different faces of the Golgi complex, are composed of unique sets of membrane proteins some of which are exposed on the cytoplasmic face of the granules.

The effect of heat treatment and skimming on precipitate formation in caprine and bovine milks

2014 ◽  
Vol 82 (1) ◽  
pp. 22-28 ◽  
Author(s):  
Zorana N Miloradovic ◽  
Nemanja V Kljajevic ◽  
Snezana T Jovanovic ◽  
Tanja R Vucic ◽  
Ognjen D Macej
Keyword(s):  
Heat Treatment ◽  
Centrifugal Force ◽  
Colloidal Stability ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bovine Milk ◽  
Protein Composition ◽  
Heat Stability ◽  
Protein Loss ◽  
Caprine Milk

Caprine and bovine milks have a similar overall gross composition, but vary considerably in the ratios of their casein components. These differences in colloidal casein micelles could affect directly or indirectly the heat stability of caprine and bovine milks at their natural pH. In the present work, the differences in colloidal stability of caprine and bovine milk have been studied by analysing the effect of heat treatment and skimming on precipitation of proteins. Raw and heated milk samples (70 °C/5 min, 80°C/5 min and 90°C/5 min) were centrifuged at 600, 2000, and 4500 g. The amount of precipitate formed after skimming was measured and the protein composition of both precipitates and supernatants analysed using the SDS-PAGE (sodium dodecyl sulphate polyacrylamide gel electrophoresis) and densitometry. In caprine milk, the heat treatment prior to skimming had a statistically significant effect on protein precipitation. Centrifugal force had a statistically significant effect on amount of precipitate for both milks, but the amount was 2 to 4 times higher for caprine milk. When defatting the milk for electrophoresis, a centrifugal force of 600 g appeared to be the most appropriate, in order to avoid protein loss and a possible error in the interpretation of results. Results of this study could also serve as the basis for further investigations on adjusting the skimming conditions for caprine milk in industrial dairy processing environment.

scholarly journals Rabbit reticulocyte coated vesicles carrying the transferrin- transferrin receptor complex: I. Purification and partial characterization

Blood ◽  
1987 ◽  
Vol 70 (4) ◽  
pp. 1035-1039
Author(s):  
HR Choe ◽  
ST Moseley ◽  
J Glass ◽  
MT Nunez
Keyword(s):  
Transferrin Receptor ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Coated Vesicles ◽  
Coated Vesicle ◽  
Receptor Complex ◽  
Assembly Factor ◽  
Excellent Source

Coated vesicles bearing the transferrin-transferrin receptor complex were isolated from rabbit reticulocytes by freeze-thaw cell lysis, followed by differential centrifugation with pelleting of vesicles at 100,000 g. Electronmicroscopy demonstrated the vesicles to have the characteristic morphology of coated vesicles, including the appearance of triskelions. The protein composition of the vesicles as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis included transferrin, transferrin receptor, and proteins of apparent mol wt of approximately 180,000, 140,000, 100,000, and 47,000 daltons. The 180,000 and 100,000 mol wt proteins were identified as clathrin and coated vesicle assembly factor proteins, respectively, by Western blot analyses. The vesicles had a Mg2+-dependent ATPase with a specific activity of approximately 8.5 nmoles ATP converted/min/mg vesicle protein. The vesicles could acidify the intravesicular space, as evidenced by the stimulation of the Mg2+-ATPase by the protonophore FCCP. Reticulocytes appear to be an excellent source of coated vesicles and as such should provide a model for studying the endocytosis of transferrin and the steps of iron uptake that proceed in these vesicles.

scholarly journals Quantitative relationship between Heinz body formation and red blood cell deformability [see comments]

Blood ◽  
1986 ◽  
Vol 68 (6) ◽  
pp. 1376-1383 ◽  
Author(s):  
WH Reinhart ◽  
LP Sung ◽  
S Chien
Keyword(s):  
Oxidative Damage ◽  
Membrane Surface ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Quantitative Relationship ◽  
Cell Deformability ◽  
Body Formation ◽  
Heinz Bodies ◽  
Heinz Body

Abstract The ultimate cause of destruction of red blood cells (RBCs) after oxidative damage with Heinz body formation is not well understood. We correlated the changes in RBC morphology and membrane protein composition after oxidant treatment with the alterations in deformability of whole cells and cell membranes. The incubation of RBCs with phenylhydrazine concentrations of 0.3 to 100 mg/dL at 37 degrees C for one hour led to a dose-dependent formation of Heinz bodies, ranging from isolated Heinz bodies at 1 mg/dL to a confluent coating of the inner membrane surface at 100 mg/dL phenylhydrazine. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of a large quantity of hemoglobin bound to the ghost membrane of treated RBCs. Electrophoresis with and without dithiothreitol indicated that disulfide bridges are abundant between hemoglobin molecules and are also present among membrane proteins but are not the major bond between hemoglobin and membrane. Changes of spectrin, ankyrin, band 3, and band 6 and the appearance of a 260,000-dalton complex were also observed. With phenylhydrazine concentrations below 30 mg/dL, even in the presence of multiple Heinz bodies, the RBC deformability measured by filtration through 2.6-, 4.5-, and 6.8-microns pores and the membrane deformability determined by a filter aspiration technique were not altered. With 100 mg/dL phenylhydrazine, when the entire membrane was coated with Heinz bodies, RBC filterability and membrane deformability were drastically reduced. These results indicate that oxidative damage of RBCs with discrete Heinz body formation causes focal membrane rigidification but does not affect the global cellular deformability until the Heinz bodies nearly cover the entire cell endoface.

Evaluation of wheat endosperm protein fingerprints as indices of Udon-noodle making quality

2001 ◽  
Vol 52 (9) ◽  
pp. 919
Author(s):  
H. Nakamura
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Protein Band ◽  
Eating Quality ◽  
Endosperm Protein ◽  
Wheat Lines ◽  
Noodle Quality

Hexaploid wheat (Triticum aestivum) endosperm protein fingerprints were used to determine the indices of Japanese soft Udon-noodle quality. The endosperm proteins of Japanese Udon wheat lines were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine differences between them in protein composition in two soil environments. The differences between the lines included differences in the composition of the endosperm with regard to the 53 kDa protein band or high-molecular-weight glutenin subunit (HMW-GS) 2* and in the sensory viscoelasticity score of cooked noodles, which is related to eating-quality in Japanese Udon wheats. One line (Kanto 107) showed variation for the presence of the 53 kDa and HMW-GS 2* bands between environments.

Human parotid saliva protein composition: dependence on physiological factors

1982 ◽  
Vol 242 (3) ◽  
pp. G231-G236 ◽  
Author(s):  
S. G. Oberg ◽  
K. T. Izutsu ◽  
E. L. Truelove
Keyword(s):  
Protein Concentration ◽  
Composition Dependence ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Parotid Saliva ◽  
Total Protein Concentration ◽  
Physiological Factors ◽  
Feeding Effects ◽  
Human Parotid Saliva

The relative concentrations of the major proteins in human parotid saliva as measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis varied greatly between the six individuals included in this study but were remarkably constant for a given individual. Individual relative parotid protein concentrations differed in salivas collected under unstimulated and stimulated conditions but were at least partially independent from circadian and feeding effects. In addition, the relative concentrations of certain salivary proteins decreased with continued lemon-drop stimulation. A total of 29 different bands was composited from the six subjects. Five of the bands had mobilities corresponding with those of calibration proteins selected for their known occurrence in parotid saliva. Only those proteins comprising at least 0.75% of the total protein concentration were detected. Relative protein concentrations of parotid saliva samples collected 12 mo apart from given individuals were identical.

Identification and characterization of outer membrane fragments released by Aeromonas sp.

1980 ◽  
Vol 58 (10) ◽  
pp. 1018-1025 ◽  
Author(s):  
S. MacIntyre ◽  
T. J. Trust ◽  
J. T. Buckley
Keyword(s):  
Outer Membrane ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cholesterol Acyltransferase ◽  
Gel Filtration ◽  
Protein Composition ◽  
Aeromonas Salmonicida ◽  
Membrane Structure And Function ◽  
And Function

Aeromonas hydrophila and Aeromonas salmonicida were shown to release "blebs" or fragments averaging 20–30 nm in diameter. The protein composition of the fragments was very similar to that of the corresponding outer membrane by sodium dodecyl sulphate – polyacrylamide gel electrophoresis and the fragments were shown to contain phospholipid and lipopolysaccharide. The results therefore indicate that the blebs are derived from the outer membrane of these organisms. Fragments isolated directly by differential ultracentrifugation were indistinguishable from fragments isolated by salt fractionation and gel filtration in chemical composition, protein composition, and density. However fragments isolated directly contained much less glycerophospholipid–cholesterol acyltransferase than those isolated by salt fractionation.The potential usefulness of membrane fragments to the bacteria and as a tool in the study of outer membrane structure and function is discussed.

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