scholarly journals Protein analysis in mucopolysaccharide-containing unicellular Colpoda cucullus by two-dimensional electrophoresis using SDS and Tween 80

2014 ◽  
Vol 58 (2) ◽  
pp. 43-45
Author(s):  
Yoichiro Sogame ◽  
Tatsuomi Matsuoka
2007 ◽  
Vol 79 (15) ◽  
pp. 5730-5739 ◽  
Author(s):  
Atsunori Hiratsuka ◽  
Hideki Kinoshita ◽  
Yuji Maruo ◽  
Katsuyoshi Takahashi ◽  
Satonari Akutsu ◽  
...  

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.


2012 ◽  
Vol 18 (5) ◽  
pp. 819 ◽  
Author(s):  
Yanhua YANG ◽  
Weitong CUI ◽  
Xiaoyong LIU ◽  
Keming ZHU ◽  
Keping CHEN

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