Fully Automated Two-Dimensional Electrophoresis System for High-Throughput Protein Analysis

2007 ◽  
Vol 79 (15) ◽  
pp. 5730-5739 ◽  
Author(s):  
Atsunori Hiratsuka ◽  
Hideki Kinoshita ◽  
Yuji Maruo ◽  
Katsuyoshi Takahashi ◽  
Satonari Akutsu ◽  
...  
1988 ◽  
Vol 173 (2) ◽  
pp. 241-245 ◽  
Author(s):  
Dipak B. Datta ◽  
Li-Ming Changchien ◽  
Concepcion R. Nierras ◽  
William A. Strycharz ◽  
Gary R. Craven

PROTEOMICS ◽  
2005 ◽  
Vol 5 (9) ◽  
pp. 2315-2318 ◽  
Author(s):  
Graeme Smith ◽  
Derek Barratt ◽  
Rachel Rowlinson ◽  
Janice Nickson ◽  
Robert Tonge

1981 ◽  
Vol 27 (11) ◽  
pp. 1807-1820 ◽  
Author(s):  
N L Anderson ◽  
J Taylor ◽  
A E Scandora ◽  
B P Coulter ◽  
N G Anderson

Abstract We describe here a computer system for the analysis of high-resolution two-dimensional gel-electrophoresis patterns, with some initial applications. The system (called TYCHO) comprises programs for image acquisition, background subtraction and smoothing, spot detection, gaussian spot modeling, and pattern matching and comparison. It is based on a conventional minicomputer, but makes extensive use of a high-speed array processor in the image-processing and -modeling steps. Used in concert with the ISO-DALT two-dimensional electrophoresis system (Anal. Biochem. 85:331-354, 1978), TYCHO allows quantitative measurement of hundreds of proteins in complex biological samples, and constitutes the initial data-reduction system required for work towards a Human Protein Index.


1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.


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