Two-dimensional electrophoresis of soluble and structure-bound proteins from cultured human fibroblasts and hair root cells: Qualitative and quantitative variation

1983 ◽  
Vol 63 (3) ◽  
Author(s):  
J. Klose ◽  
I. Willers ◽  
S. Singh ◽  
H.W. Goedde
Keyword(s):  
Human Fibroblasts ◽  
Quantitative Variation ◽  
Two Dimensional ◽  
Hair Root ◽  
Root Cells ◽  
Two Dimensional Electrophoresis ◽  
Qualitative And Quantitative ◽  
Cultured Human Fibroblasts ◽  
Dimensional Electrophoresis

Qualitative and Quantitative Analyses of Bovine, Rabbit and Human Dental Pulp Glycosaminoglycans

1979 ◽  
Vol 58 (2) ◽  
pp. 646-655 ◽  
Author(s):  
Naoki Sakamoto ◽  
Hiroshi Okamoto ◽  
Kyuichiro Okuda
Keyword(s):  
Hyaluronic Acid ◽  
Dental Pulp ◽  
Two Dimensional ◽  
Dermatan Sulphate ◽  
Two Dimensional Electrophoresis ◽  
Qualitative And Quantitative ◽  
Human Dental Pulp ◽  
Quantitative Analyses ◽  
Rabbit Dental Pulp ◽  
Dimensional Electrophoresis

Bovine, rabbit and human dental pulp glycosaminoglycans were analyzed qualitatively and quantitatively using two-dimensional electrophoresis. The major components of bovine and rabbit dental pulp were chondroitin 4-sulphate and hyaluronic acid, while in the human dental pulp dermatan sulphate and chondroitin 4-sulphate were the major components.

Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub
Keyword(s):  
Sialic Acid ◽  
Polypeptide Chain ◽  
Two Dimensional ◽  
Charge Heterogeneity ◽  
Human Fibrinogen ◽  
Two Dimensional Electrophoresis ◽  
Isoelectric Points ◽  
Polypeptide Chains ◽  
Dimensional Electrophoresis ◽  
Chain Type

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.

Improvement of Two-dimensional Electrophoresis of Rice (Oryza sativaL.) Proteomics

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

Establishment of two-dimensional electrophoresis(2-DE)technique in muscle proteome of Fenneropenaeus chinensis

2013 ◽  
Vol 37 (2) ◽  
pp. 288
Author(s):  
Zhiyuan LIU ◽  
Jianrong LI ◽  
Xuepeng LI ◽  
Tingting LI ◽  
Yanbo WANG ◽  
...  
Keyword(s):  
Fenneropenaeus Chinensis ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Muscle Proteome ◽  
Dimensional Electrophoresis
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