Changes in Isoelectric Point as Affected by Anion Adsorption on Two Brazilian Oxisols

2006 ◽  
Vol 37 (9-10) ◽  
pp. 1357-1366 ◽  
Author(s):  
G. Marchi ◽  
L. R. G. Guilherme ◽  
A. C. Chang ◽  
N. Curi ◽  
M. C. Guerreiro
Keyword(s):  
Isoelectric Point ◽  
Anion Adsorption

Impedance aspects of anion adsorption on gold single crystal electrodes

1996 ◽  
Vol 414 (2) ◽  
pp. 209-220 ◽  
Author(s):  
Tamás Pajkossy ◽  
Thomas Wandlowski ◽  
Dieter M. Kolb
Keyword(s):  
Single Crystal ◽  
Anion Adsorption

Cross-Linked αsγt-Chain Hybrids in Plasma Clots Studied by 1D- and 2D Electrophoresis and Western Blotting

1993 ◽  
Vol 70 (03) ◽  
pp. 438-442 ◽  
Author(s):  
B Grøn ◽  
C Filion-Myklebust ◽  
S Bjørnsen ◽  
P Haidaris ◽  
F Brosstad
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibodies ◽  
Human Plasma ◽  
Western Blotting ◽  
Isoelectric Point ◽  
Factor Xiii ◽  
Cross Linking ◽  
2D Electrophoresis ◽  
Complex Phenomenon ◽  
Fibrinopeptide A

SummaryFibrinogen and fibrin related chains in reduced human plasma as well as the bonds interlinking partially cross-linked fibrin from plasma clots have been studied by means of 1D- and 2D electrophoresis and Western blotting. Immunovisualization of reduced plasma or partially cross-linked fibrin with monoclonal antibodies specific for the α-chains or the γ-chains have shown that several bands represent material belonging to both chains. In order to decide whether these bands constitute αγ-chain hybrids or superimposed α- and γ-chain dimers, the cross-linked material was separated according to both isoelectric point (pI) and molecular weight (MW) using Pharmacia’s Multiphor II system. Western blotting of the second dimension gels revealed that partially cross-linked fibrin contains αsγt-chain hybrids and γ- polymers, in addition to the well-known γ-dimers and α-polymers. The main αsγt-chain hybrid has a pI between that of the α- and the γ-chains, a MW of about 200 kDa and contains Aα-chains with intact fibrinopeptide A (FPA). It was also observed that soluble fibrinogen/fibrin complexes as well as partially cross-linked fibrin contain degraded α-dimers with MWs close to the γ-dimers. These findings demonstrate that factor XIII-catalyzed cross-linking of fibrin is a more complex phenomenon than earlier recognized.

A Comparison of Plasminogen Activators Derived from Rat Plasma, Primary Rat Hepatocytes and Isolated Perfused Rat Liver

1982 ◽  
Vol 47 (02) ◽  
pp. 166-172 ◽  
Author(s):  
Yoav Sharoni ◽  
Maria C Topal ◽  
Patricia R Tuttle ◽  
Henry Berger
Keyword(s):  
Rat Liver ◽  
Isoelectric Point ◽  
Rat Hepatocytes ◽  
Cell Types ◽  
Plasminogen Activators ◽  
Rat Plasma ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Molecular Weights ◽  
Physiological Relevance

SummaryOf the two cell types it was possible to culture from the dissociated rat liver, hepatocytes and Kupffer cells, only the former were fibrinolytically active. Rat hepatocytes during the first 24 hr in culture secreted two plasminogen activators with molecular weights identical to those found in rat plasma, an 80,000-dalton form (PA-80) and a 45,000-dalton form (PA-45). Partially purified preparations of plasminogen activators from both sources were subjected to isoelectric focusing (IEF) to compare characteristics further. There were three distinct peaks of PA-45 in each preparation with isoelectric points of 7.1, 7.2 and 7.4; all electrophoretic forms had the same low affinity to fibrin. PA-80 from both sources displayed similar IEF profiles with forms ranging from pH values of 7 to 8, all with the same high affinity to fibrin. The major form of PA-80 in the plasma preparation had an isoelectric point of 7.9 whereas that in the hepatocyte preparation had an isoelectric point of 7.6. The isolated perfused rat liver was also shown to produce both PA-80 and PA-45 emphasizing the physiological relevance of the findings with hepatocytes. It is concluded that in the rat hepatocytes contribute to the plasma profile with regard to the plasminogen activator content.

scholarly journals Isoelectric Point of Proteins by Differential Conductimetry

1965 ◽  
Vol 240 (4) ◽  
pp. PC1864-PC1866
Author(s):  
A.J. Sophianopoulos ◽  
E.A. Sasse
Keyword(s):  
Isoelectric Point

Enzyme Immobilization Behavior on the Surface of Hydroxyapatite Capsules under Alkaline Condition

2018 ◽  
Vol 782 ◽  
pp. 21-26
Author(s):  
Takeshi Yabutsuka ◽  
Masaya Yamamoto ◽  
Shigeomi Takai ◽  
Takeshi Yao
Keyword(s):  
Enzyme Immobilization ◽  
Double Layer ◽  
Isoelectric Point ◽  
Electrical Double Layer ◽  
Alkaline Condition ◽  
Bicarbonate Buffer

We prepared hydroxyapatite (HA) capsules encapsulating maghemite particles. In order to evaluate enzyme immobilization behavior of the HA capsules under alkaline condition, we immobilized five kinds of enzymes with different isoelectric point in carbonate/bicarbonate buffer (CBB, pH 10.0). When the enzymes in CBB were moderately charged, immobilization efficiency on the HA capsules showed the highest value. It was suggested that immobilization efficiency was affected according to both pI of enzyme and pH of the surrounding solution and that enzyme immobilized on the HA capsules by not only electrical double layer interactions but also ion interaction and other interactions.

Electrokinetic Potential for Characterization of Nanosctructured Solid Flat Surfaces

2013 ◽  
Vol 25 ◽  
pp. 31-39 ◽  
Author(s):  
Zdeňka Kolská ◽  
Nikola Slepičková Kasálková ◽  
Jakub Siegel ◽  
Václav Švorčík
Keyword(s):  
Zeta Potential ◽  
Isoelectric Point ◽  
Electrokinetic Potential ◽  
Characteristic Parameter ◽  
Metal Nanostructures ◽  
Gold Deposition ◽  
Fast Analysis ◽  
Flat Surfaces ◽  
Acceptable Method ◽  
Point Determination

Electrokinetic potential (zeta potential) is a characteristic parameter for description of the surface chemistry of solid flat materials and it can be used for a fast analysis of materials modified by different chemical or physical methods. Due to its sensitivity, zeta potential is able to distinguish surface modified by coating with monolayers of various materials or nanostructures created after plasma treatment. Also metal nanostructures deposited on surfaces can be characterized by zeta potential. It can also be used for isoelectric point determination of materials. We present data on zeta potential in 0.001 mol/dm3 KCl at constant pH7.0 and also in pH range (2.5-7.0) for isoelectric point determination for pristine polymers PET, PTFE, PS, LDPE, HDPE, PLLA, PVF, PVDF, PMP and polyimides (Upilex R, Upilex S, Kapton). The zeta potential of selected polymers, modified by plasma and by chemical coatings (e.g. by biphenyldithiol or polyethyleneglycol) or by gold deposition was measured too. Zeta potentials of these modified materials were also studied to confirmation that electrokinetic analysis is acceptable method for their fast description.

scholarly journals THE ISOELECTRIC POINT OF RED BLOOD CELLS AND ITS RELATION TO AGGLUTINATION

1921 ◽  
Vol 3 (3) ◽  
pp. 309-323 ◽  
Author(s):  
Calvin B. Coulter
Keyword(s):  
Red Blood Cells ◽  
Isoelectric Point ◽  
Blood Cells ◽  
Inorganic Ions ◽  
Immune Serum ◽  
Ion Concentration ◽  
Normal Cells ◽  
Hydrogen Ion Concentration ◽  
Alkaline Side ◽  
Chlorine Ions

1. The movement of normal and sensitized red blood cells in the electric field is a function of the hydrogen ion concentration. The isoelectric point, at which no movement occurs, corresponds with pH 4.6. 2. On the alkaline side of the isoelectric point the charge carried is negative and increases with the alkalinity. On the acid side the charge is positive and increases with the acidity. 3. On the alkaline side at least the charge carried by sensitized cells is smaller and increases less rapidly with the alkalinity than the charge of normal cells. 4. Both normal and sensitized cells combine chemically with inorganic ions, and the isoelectric point is a turning point for this chemical behavior. On the acid side the cells combine with the hydrogen and chlorine ions, and in much larger amount than on the alkaline side; on the alkaline side the cells combine with a cation (Ba), and in larger amount than on the acid side. This behavior corresponds with that found by Loeb for gelatin. 5. The optimum for agglutination of normal cells is at pH 4.75, so that at this point the cells exist most nearly pure, or least combined with anion and cation. 6. The optimum for agglutination of sensitized cells is at pH 5.3. This point is probably connected with the optimum for flocculation of the immune serum body.

scholarly journals THE ISOELECTRIC ZONE OF TYPHOID AGGLUTININ

1926 ◽  
Vol 9 (3) ◽  
pp. 345-350 ◽  
Author(s):  
R. Ottenberg ◽  
F. A. Stenbuck
Keyword(s):  
Isoelectric Point

The isoelectric point of typhoid agglutinin lies between pH 4.4 and pH 4.6.

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