scholarly journals Proteomic analysis of cold adaptation in a Siberian permafrost bacterium - Exiguobacterium sibiricum 255-15 by two-dimensional liquid separation coupled with mass spectrometry

PROTEOMICS ◽  
2006 ◽  
Vol 6 (19) ◽  
pp. 5221-5233 ◽  
Author(s):  
Yinghua Qiu ◽  
Sophia Kathariou ◽  
David M. Lubman
Keyword(s):  
Mass Spectrometry ◽  
Proteomic Analysis ◽  
Cold Adaptation ◽  
Two Dimensional ◽  
Liquid Separation ◽  
Siberian Permafrost

Proteomic analysis ofCandida magnoliae strains by two-dimensional gel electrophoresis and mass spectrometry

PROTEOMICS ◽  
2003 ◽  
Vol 3 (12) ◽  
pp. 2330-2338 ◽  
Author(s):  
Do-Yup Lee ◽  
Yong-Cheol Park ◽  
Hyo-Jin Kim ◽  
Yeon-Woo Ryu ◽  
Jin-Ho Seo
Keyword(s):  
Mass Spectrometry ◽  
Proteomic Analysis ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Proteomic analysis of melanoma-derived exosomes by two-dimensional polyacrylamide gel electrophoresis and mass spectrometry

PROTEOMICS ◽  
2004 ◽  
Vol 4 (12) ◽  
pp. 4019-4031 ◽  
Author(s):  
Rainy Mears ◽  
Rachel A. Craven ◽  
Sarah Hanrahan ◽  
Nick Totty ◽  
Carol Upton ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Proteomic Analysis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional

scholarly journals Two-dimensional gel electrophoresis to identify arcelins from Phaseolus vulgaris with inmuno-proteomic analysis

2018 ◽  
Vol 36 (2) ◽  
pp. 114-119
Author(s):  
Carolina Bernal ◽  
Daynet Sosa ◽  
Iván Galindo-Castro ◽  
Nardy Diez
Keyword(s):  
Mass Spectrometry ◽  
Proteomic Analysis ◽  
Gel Electrophoresis ◽  
Mass Spectrometry Analysis ◽  
Two Dimensional ◽  
Storage Pests ◽  
Molecular Weight Range ◽  
Two Dimensional Gel Electrophoresis ◽  
Breeding Programs ◽  
Spectrometry Analysis

The present study used proteomics to analyze the expression of lectin-like proteins, specifically arcelins, in P. vulgaris cultivar varieties from Venezuela. A PAGE-SDS analysis of 30 commercial accessions of P. vulgaris showed significant differences in the molecular weight range of lectin-like proteins (arcelins). Eight different accessions were selected based on their electroforetic mobility for the proteomic analysis. Arcelin immuno-detection of two dimentional electrophoresed proteins was used to easily display the different arcelin proteomic profiles of the studied accessions. Mass spectrometry analysis confirmed the arcelin nature of these proteins. This is the first report on arcelin evaluation of the Venezuelan germoplasm of P. vulgaris with the aim of enhancing breeding programs by identifying accession materials with resistance to bean storage pests.

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