scholarly journals  Analysis of whole cell protein profiles of Salmonella serovars isolated from chicken, turkey and sheep faeces by SDS-PAGE

2010 ◽  
Vol 55 (No. 6) ◽  
pp. 259-263 ◽  
Author(s):  
A. Aksakal
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Visual Assessment ◽  
Cell Protein ◽  
Protein Profiles ◽  
Whole Cell ◽  
Sds Page ◽  
Molecular Masses ◽  
Whole Cell Protein ◽  
Salmonella Serovars

This study was carried out to determine the whole cell protein profiles of Salmonella serovars from chicken, turkey and sheep faeces by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). A total of 34 Salmonella strains were included in the study, 14 of them were isolated from chicken, 14 from turkey and six from sheep. SDS-PAGE was carried out using 12% (w/v) separating and 4% (w/v) stacking gels. The results showed more than 30 protein bands ranging in size from 97 kDa (kilodaltons) to below 14.4 kDa as determined by visual assessment of their approximate molecular masses. Protein bands of 78.1, 51.2, 41.5, 37.3, 35.1, 33.9, 30.7, 27.6, 25.4, and 24 kDa were detected in all Salmonella serovars. Salmonella strains used in this study were closely related and could not be differentiated depending on the whole cell protein profiles using SDS-PAGE.

scholarly journals Analysis of Whole Cell Protein Profiles by SDS-PAGE to Identify Indigenous Cellulose-producer Acetic Acid Bacteria

2017 ◽  
Vol 21 (2) ◽  
pp. 86
Author(s):  
Sarkono Sarkono ◽  
Soekarti Moeljopawiro ◽  
Bambang Setiaji ◽  
Langkah Sembiring
Keyword(s):  
Acetic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Acetic Acid Bacteria ◽  
Cellular Protein ◽  
Cell Protein ◽  
Phenotypic Traits ◽  
Protein Profiles ◽  
Bacterial Isolates ◽  
Sds Page

This study was carried out to analyze the suitability of the identification of four indigenous cellulose-producing acetic acid bacterial isolates (ANG29, KRE65, ANG32 and SAL53) based on the analysis of whole cellular protein profiles against identification based on phenotypic traits. Whole cellular protein profiles were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) method. The whole cellular protein profiles obtained from sample isolates, were compared with reference isolates for species identification. The results showed that based on visual observations can be determined as much as 12 bands of protein with a molecular weight of 19,099 KDa up to 132.182 KDa. Based on the analysis of protein bands were detected visually, fourth indigenous cellulose- producing acetic acid bacterial isolates in the study had a higher similarity profile to the reference strain Gluconacetobacter xylinus BTCC 769 compared with other reference strains namely G. hansenii NBRC 14820T. This condition is consistent with the results of the identification of fourth cellulose producing acetic acid bacterial isolates based on phenotypic traits. Thus, the whole cellular protein profiles by SDS-PAGE technique can be used as a one of method to identification of cellulose producing acetic acid bacterial isolates.

A simple and rapid method for the differentiation and identification of thermophilic bacteria

2006 ◽  
Vol 52 (8) ◽  
pp. 753-758 ◽  
Author(s):  
Bin Liu ◽  
Hebin Li ◽  
Suijie Wu ◽  
Xiaobo Zhang ◽  
Lianhui Xie
Keyword(s):  
Hot Spring ◽  
Thermophilic Bacteria ◽  
Random Amplified Polymorphic Dna ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cell Protein ◽  
Protein Patterns ◽  
Simple Method ◽  
Whole Cell ◽  
Sds Page

In total, 170 strains of thermophilic bacteria were isolated from deep-sea hydrothermal fields in the Pacific Ocean and a hot spring in Xiamen of China. To facilitate the identification of thermophilic strains, sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE) of whole-cell proteins of these strains was first performed. The results showed that there exist four different protein patterns, indicating that the 170 strains might belong to four species or genera. The RAPD (random amplified polymorphic DNA) profiles of nine representative strains were consistent with those of SDS–PAGE. To further identify the species of the nine strains, their 16S rDNA sequences were analyzed. The results showed that the nine strains fell into four species of three genera, which was the same as revealed by SDS–PAGE. Therefore, SDS–PAGE of whole-cell proteins could be used as a rapid and simple method for the discrimination of thermophilic bacteria as the first step of species identification.Key words: thermophilic bacteria, SDS–PAGE, whole-cell protein, discrimination.

scholarly journals Differentiation of Pathogenic Groups of Xylella fastidiosa Strains with Whole-Cell Protein Profiles

Plant Disease ◽  
2002 ◽  
Vol 86 (8) ◽  
pp. 875-879 ◽  
Author(s):  
R. L. Wichman ◽  
D. L. Hopkins
Keyword(s):  
Xylella Fastidiosa ◽  
Sodium Dodecyl ◽  
Mass Range ◽  
Cell Protein ◽  
Pierce's Disease ◽  
Protein Profiles ◽  
Whole Cell ◽  
Leaf Scorch ◽  
Pierce’S Disease ◽  
Whole Cell Protein

Whole-cell protein analyses of 75 Xylella fastidiosa strains by sodium dodecyl sulfatepolyacrylamide gel electrophoresis were compared, and variations in the protein banding patterns among the strains were observed. Based on the presence, absence, or difference in intensity of 10 protein bands within the 21.5 to 45.0 kDa molecular mass range, the strains could be subdivided into four distinct pathogenic groups and two miscellaneous groups whose members were pathogenic to various different hosts. Group 1 was the Pierce's disease of grapevine pathogenic group. Although 4 of these 45 strains had hosts of origin other than grapevine, they all produced Pierce's disease symptoms. Uniform, distinct protein profiles also occurred with group 2 (elderberry leaf scorch strains), group 3 (oak leaf scorch strains), and group 4 (oleander leaf scorch strains). Groups 5 and 6 were made up of strains pathogenic to almond, blackberry, lupine, mulberry, periwinkle, elm, and plum. Thus, whole-cell protein analysis was shown to be a rapid and consistent method for identifying four pathogenic groups of X. fastidiosa strains.

Verification of Nodulation Ability of Strains Isolated fromMimosaspp. Nodules Using Whole Cell Protein SDS-PAGE Molecular Marker Method*

2010 ◽  
Vol 2009 (5) ◽  
pp. 719-723
Author(s):  
Xiaoyun LIU ◽  
Bin ZHANG ◽  
Wei WU ◽  
Qiaoxian LI
Keyword(s):  
Molecular Marker ◽  
Cell Protein ◽  
Whole Cell ◽  
Sds Page ◽  
Whole Cell Protein

Protein Expression in Vibrio parahaemolyticus 690 Subjected to Sublethal Heat and Ethanol Shock Treatments

2008 ◽  
Vol 71 (11) ◽  
pp. 2289-2294 ◽  
Author(s):  
MING-LUN CHIANG ◽  
WEI-LI HO ◽  
ROCH-CHUI YU ◽  
CHENG-CHUN CHOU
Keyword(s):  
Heat Shock ◽  
Vibrio Parahaemolyticus ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Test Organism ◽  
Protein Patterns ◽  
One Dimensional ◽  
Sds Page ◽  
Molecular Masses ◽  
Stressed Cells

Cells of Vibrio parahaemolyticus 690 were subjected either to heat shock at 42°C for 45 min or to ethanol shock in the presence of 5% ethanol for 60 min. The protein profiles of the unstressed and stressed V. parahaemolyticus cells were compared. Additionally, the induction of DnaK- and GroEL-like proteins in the unstressed and stressed cells of V. parahaemolyticus was also examined. Analysis with one-dimensional sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) indicated that three proteins with molecular masses of 93, 77, and 58 kDa were induced by both heat shock and ethanol shock. The protein patterns revealed by two-dimensional electrophoresis were more detailed than those revealed by one-dimensional SDS-PAGE. It was found that heat shock and ethanol shock affected the expression of a total of 28 proteins. Among them, four proteins with molecular masses of 94, 32.1, 26.7, and 25.7 kDa were enhanced by both heat shock and ethanol shock. Furthermore, immunoblot analysis showed the presence of a GroEL-like protein with a molecular mass of 61 kDa in the test organism, with the heat-shocked and ethanol-shocked cells producing a GroEL-like protein in a larger quantity than the unstressed cells. However, DnaK-like protein was not detectable in either the unstressed or the stressed cells.

Whole-cell protein and ITS rDNA profiles as diagnostic tools to discriminate Fusarium avenaceum intraspecific variability and associated virulence

2009 ◽  
Vol 55 (2) ◽  
pp. 117-125 ◽  
Author(s):  
V. Vujanovic ◽  
S. Vidovic ◽  
M. R. Fernandez ◽  
P. Daida ◽  
D. Korber
Keyword(s):  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Intraspecific Variability ◽  
Fusarium Avenaceum ◽  
Cell Protein ◽  
Diagnostic Tools ◽  
Group Method ◽  
Head Blight ◽  
Sds Page

A total of 91 isolates of Fusarium avenaceum were regrouped into 15 phenotypes and 10 vegetative compatibility groups showing specific one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis (1-D SDS–PAGE) protein profiles and less-specific internal transcribed spacer rDNA profiles. Each isolate possessed reproducible signature protein bands. Indeed, the unweighted pair group method with arithmetic averages clustering revealed that the protein profile of each group of isolates correlated with fungus virulence. The use of SDS–PAGE offers a simple and sensitive technique for routine differentiation between pathogenic and nonpathogenic isolates within unknown F. avenaceum populations. The discovery has significant implications for risk assessment of cereal yield to ensure food and feed safety. This low-cost approach has the potential to be optimized and extended to a broad spectrum of Fusarium head blight pathogens.

scholarly journals Digestibility of β-lactoglobulin following cross-linking by trametes versicolor laccase and apple polyphenols

2011 ◽  
Vol 76 (6) ◽  
pp. 847-855 ◽  
Author(s):  
Ziyad Tantoush ◽  
Luka Mihajlovic ◽  
Bojana Kravic ◽  
Jana Ognjenovic ◽  
Ratko Jankov ◽  
...  
Keyword(s):  
Nutritional Value ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cross Linking ◽  
Allergenic Potential ◽  
Sds Page ◽  
Molecular Masses ◽  
Quercetin Glycosides ◽  
Phenolic Extract ◽  
Β Lactoglobulin

?-Lactoglobulin (BLG) is an important nutrient of dairy products and an important allergen in cow?s milk allergy. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an apple phenolic extract (APE) and to characterize the obtained products for their digestibility by pepsin and pancreatin. The composition of the apple phenolics used for cross-linking was determined by LC-ESE-MS. The apple phenolic extract contained significant amounts of quercetin glycosides, catechins and chlorogenic acid. The laccase cross-linked BLG in the presence of apple phenolics. The polymerization rendered the protein insoluble in the reaction mixture. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the cross-linking reaction mixture revealed a heterogeneous mixture of high molecular masses (cross-linked BLG), with a fraction of the BLG remaining monomeric. Enzymatic processing of BLG by laccase and apple polyphenols as mediators can decrease the bi-phasal pepsin- pancreatin digestibility of the monomeric and cross-linked protein, thus decreasing its nutritional value. In addition, reduced BLG digestibility can decrease its allergenic potential. Apple polyphenols can find usage in the creation of new, more functional food products, designed to prevent obesity and hypersensitivity-related disorders.

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