The application of whole-cell protein electrophoresis for the classification and identification of basidiomycetous yeast species

1992 ◽  
Vol 61 (1) ◽  
pp. 69-78 ◽  
Author(s):  
Marc Vancanneyt ◽  
Eddy Van Lerberge ◽  
Jean-Francois Berny ◽  
Gregoire L. Hennebert ◽  
Karel Kersters
Keyword(s):  
Yeast Species ◽  
Protein Electrophoresis ◽  
Basidiomycetous Yeast ◽  
Cell Protein ◽  
Whole Cell ◽  
Whole Cell Protein

Clusterization of halophilic and halotolerant eubacteria using whole-cell protein electrophoresis data

Microbiology ◽  
2000 ◽  
Vol 69 (5) ◽  
pp. 582-587 ◽  
Author(s):  
S. A. Bykova ◽  
I. S. Zvyagintseva ◽  
D. S. Akhlynin ◽  
S. S. Belyaev ◽  
V. F. Gal’chenko
Keyword(s):  
Protein Electrophoresis ◽  
Cell Protein ◽  
Whole Cell ◽  
Whole Cell Protein

Differentiation of Yeast Species Based on Electrophoretic Whole-Cell Protein Patterns

1991 ◽  
Vol 14 (1) ◽  
pp. 23-32 ◽  
Author(s):  
M. Vancanneyt ◽  
B. Pot ◽  
G. Hennebert ◽  
K. Kersters
Keyword(s):  
Yeast Species ◽  
Cell Protein ◽  
Protein Patterns ◽  
Whole Cell ◽  
Whole Cell Protein

Preliminary screening for toxin genes amongst stock cultures of Clostridium perfringens strains isolated from dogs and calves

2014 ◽  
Vol 4 (3) ◽  
pp. 127-132
Author(s):  
Egwari L. O. ◽  
Oghogho E. S. ◽  
Okwumabua O. E. ◽  
Oniha M. I.
Keyword(s):  
Clostridium Perfringens ◽  
Protein Profile ◽  
Animal Origin ◽  
Cell Protein ◽  
Toxin Gene ◽  
Whole Cell ◽  
University Of Wisconsin ◽  
Gene Type ◽  
Whole Cell Protein ◽  
Gene 4

The spectrum of Clostridium perfringens infections ranges from food toxinosis to myonecrosis. In the current study, whole cell protein and toxin gene types were profiled in 12 randomly selected C. perfringens veterinary stock cultures from the University of Wisconsin, Madison to determine epidemio-logical similarity, or diversity amongst strains of animal origin. Whole cell protein analysis was done by SDS-PAGE while toxin gene typing was achieved by extracting DNA by boiling, DNA concentration and purity was determined by spectrophotometer and nanodrop while separation was carried out by checking it on gel electrophoresis. Multiplex PCR was used to identify the toxigenic gene-type. C. perfringens B and C. perfringens EE with established profiles were used as control strains. Isolates typed included strains cp 296, 309, 12872 (from dogs) and 304, 305, 306, 341, 342, 10754, 12218-2, 12218-3, 12473 (from calves). All 12 strains possess the cpa gene, 4 strains have cpb2, 3 strains etx, 2 strains positive for cpe and 1 for cpb. None of the strains carries the itx gene. Two strains have only cpa gene however no strains has more than two toxin gene types, with cpa-cpb2 combination be-ing more frequent. C. perfringens 305 (etx and cpa) and 342 (cpe and cpa) shared the same protein profile but belong to different toxinotype. It is evi-dent that the cpa gene is a marker for all C. perfringens strains, and similarity in protein profile is not sine qua non for toxin gene type.

scholarly journals Partial Proteome Map of Campylobacter Jejuni Strain Nctc11168 by Gel-Free Proteomics Analysis

2014 ◽  
Vol 2 (4) ◽  
pp. 464-477
Author(s):  
Zilun Shi ◽  
Chris Dawson ◽  
Stephen L.W. On ◽  
Malik Altaf Hussain
Keyword(s):  
Campylobacter Jejuni ◽  
Foodborne Pathogen ◽  
Brain Heart Infusion ◽  
Cell Protein ◽  
Absolute Quantitation ◽  
Whole Cell ◽  
Itraq Analysis ◽  
Proteomic Approach ◽  
Whole Cell Protein ◽  
Isobaric Tags

A proteome map of the foodborne pathogen Campylobacter jejuni NCTC11168 was analyzed using a state-of-the-art gel-free proteomic approach for the first time. A whole cell protein extract was prepared from the C. jejuni strain NCTC11168 grown in brain heart infusion (BHI) broth at 42°C under microaerobic conditions. A gel-free technique using isobaric tags for relative and absolute quantitation (iTRAQ) was employed to create a protein expression profile of the strain. Liquid chromatography-mass spectrometry (LC-MS/MS) was used to identify the proteins. Protein functionalities were searched to classify them. A total of 235 proteins were identified in the whole cell protein fraction of C. jejuni NCTC11168 cells using iTRAQ analysis. Functional grouping of the identified proteins showed that forty percent of these proteins were associated with energy metabolism, protein synthesis and genetic information processing. iTRAQ was faster, easier and proved more sensitive than two-dimensional gel-based proteomics approaches previously applied to C. jejuni, making it an attractive tool for further studies of cellular physiological response. DOI: http://dx.doi.org/10.3126/ijasbt.v2i4.11253  Int J Appl Sci Biotechnol, Vol. 2(4): 464-477 

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