Influence of surface charge density on protein adsorption on polymeric nanoparticles: analysis by two-dimensional electrophoresis

2002 ◽  
Vol 54 (2) ◽  
pp. 165-170 ◽  
Author(s):  
Andrea Gessner ◽  
Antje Lieske ◽  
Bernd R Paulke ◽  
Rainer H Müller
Keyword(s):  
Charge Density ◽  
Surface Charge ◽  
Protein Adsorption ◽  
Surface Charge Density ◽  
Polymeric Nanoparticles ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

scholarly journals Controlling protein adsorption modes electrostatically

Soft Matter ◽  
2020 ◽  
Vol 16 (22) ◽  
pp. 5224-5232
Author(s):  
Yuba Raj Dahal ◽  
Monica Olvera de la Cruz
Keyword(s):  
Charge Density ◽  
Surface Charge ◽  
Protein Adsorption ◽  
Surface Charge Density ◽  
Ion Concentration ◽  
Charged Surfaces ◽  
P Protein

Protein adsorption modes on charged surfaces determined by surface charge density and explicit ion concentration.

scholarly journals On triple trigonometrical equations

1973 ◽  
Vol 14 (2) ◽  
pp. 174-178 ◽  
Author(s):  
B. M. Singh
Keyword(s):  
Exact Solution ◽  
Charge Density ◽  
Surface Charge ◽  
Electrostatic Potential ◽  
Surface Charge Density ◽  
Equal Length ◽  
Two Dimensional ◽  
Electrostatic Problem ◽  
Unit Depth

An exact solution of triple trigonometrical equations is obtained by using the finiteHilbert transform. The solution of these equations is used to solve a two-dimensional electrostatic problem. The problem of determining the electrostatic potential due to two parallel coplanar strips of equal length, charged to equal and opposite potentials, each parallel to and equidistant from an earthed strip, is considered. Both the charged strips lie along the x-axis and they are equally spaced with respect to the y-axis. Finally the expression for the surface charge density (per unit depth) of the strip is derived

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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