Proteins of rat serum: III. Gender-related differences in protein concentration under baseline conditions and upon experimental inflammation as evaluated by two-dimensional electrophoresis

2007 ◽  
pp. 256-265
Author(s):  
Ingrid Miller ◽  
Paul Haynes ◽  
Ivano Eberini ◽  
Manfred Gemeiner ◽  
Ruedi Aebersold ◽  
...  
Keyword(s):  
Protein Concentration ◽  
Two Dimensional ◽  
Rat Serum ◽  
Two Dimensional Electrophoresis ◽  
Experimental Inflammation ◽  
Baseline Conditions ◽  
Dimensional Electrophoresis

scholarly journals Evaluation of six different protocols for protein extraction from rice young panicles by two-dimensional electrophoresis

2020 ◽  
Author(s):  
Xiaoping Huang ◽  
Hui-wen Zhou
Keyword(s):  
Protein Concentration ◽  
Protein Extraction ◽  
Image Resolution ◽  
Plant Tissues ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Molecular Weight Range ◽  
Two Dimensional Electrophoresis ◽  
Phenol Extraction ◽  
Dimensional Electrophoresis

Abstract Background: For most reported proteomics approaches, protein extraction are of crucial importance for optimal results. However, extraction of protein from plant tissues still exist great challenges due to low protein content and many secondary metabolites that prominently interfering with isoelectric focusing. Up to now, no attempts are focused on comparison of protein extraction from rice young panicles.Methods: To establish a higher efficiency protein extraction protocol suited for two-dimensional electrophoresis in rice young panicles, six protocols for protein preparation were evaluated in terms of protein concentration, the molecular weight range of protein, gel image resolution, the number of protein spots: 1) Phenol extraction; 2) Mg/Nonidet P-40 (NP-40) extraction; 3) Tris-Base/acetone extraction; 4) SDS extraction; 5) trichloroacetic acid (TCA)/acetone/phenol extraction; 6) TCA/acetone precipitation.Results: The result explicitly demonstrated that TCA/acetone/phenol method provided a high-enhanced protein extraction efficacy from rice young panicles than other protocols in terms of the protein concentration (9.79±0.23 SD), the most comprehensive proteins (10 KDa to 150 KDa), the maximum number of protein spots (450±53 SD), the greater gel image resolution and spot abundance. In addition, these methods also generated remarkably differential 2-DE protein patterns. Twenty-nine of 30 visible differentially extracted proteins were identified by MS analysis and were divided into eight categories. Prediction for protein subcellular localization and grand average of hydropathy (GRAVY) analysis showed that certain special proteins respectively necessitate different extraction methods due to different physicochemical properties of each protocol.Conclusions: Overall, this paper will facilitate to provide a cornerstone of comparative proteomic analysis from rice young panicles, including other complicated plant tissues.

Proteins of rat serum: II. Influence of some biological parameters of the two-dimensional electrophoresis pattern

1998 ◽  
Vol 19 (8-9) ◽  
pp. 1493-1500 ◽  
Author(s):  
Ingrid Miller ◽  
Paul Haynes ◽  
Manfred Gemeiner ◽  
Ruedi Aebersold ◽  
Cristina Manzoni ◽  
...  
Keyword(s):  
Two Dimensional ◽  
Biological Parameters ◽  
Rat Serum ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Electrophoresis Pattern

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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