Studies on the procedure for the construction of cellular protein databases employing micro two-dimensional electrophoresis: An HL-60 protein database

1995 ◽  
Vol 16 (1) ◽  
pp. 407-422 ◽  
Author(s):  
Takashi Manabe ◽  
Hideko Yamamoto ◽  
Makoto Kawai
Keyword(s):  
Cellular Protein ◽  
Two Dimensional ◽  
Protein Database ◽  
Protein Databases ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Construction of aFrancisella tularensis two-dimensional electrophoresis protein database

PROTEOMICS ◽  
2001 ◽  
Vol 1 (4) ◽  
pp. 508-515 ◽  
Author(s):  
Lenka Hernychová ◽  
Jiří Stulík ◽  
Petr Halada ◽  
Aleš Macela ◽  
Michal Kroča ◽  
...  
Keyword(s):  
Two Dimensional ◽  
Protein Database ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Detection of Differentially Expressed Proteins of Capsulation-Resistant and Sensitive Osteosarcoma Tissue

2013 ◽  
Vol 756-759 ◽  
pp. 4553-4556
Author(s):  
Li Heng Zhang ◽  
Liang Li
Keyword(s):  
Mass Spectrometry ◽  
Differentially Expressed ◽  
Two Dimensional ◽  
Differentially Expressed Proteins ◽  
Tissue Samples ◽  
Chemosensitivity Testing ◽  
Protein Databases ◽  
Two Dimensional Electrophoresis ◽  
Mass Spectrometry Technology ◽  
Dimensional Electrophoresis

The tissue samples of cisplatin-resistant and sensitive patients with osteosarcoma were obtained through chemosensitivity testing before. The typical one of cisplatin-resistant and sensitive osteosarcoma tissue samples were analyzed by two-dimensional electrophoresis and the relevant differentially expressed proteins were obtained. The sequences of differentially expressed proteins were obtained through the analysis of mass spectrometry technology to be identified comparing with protein databases. It is concluded that there are differentially expressed proteins in tissue of cisplatin-resistant and sensitive osteosarcoma.

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
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