Kinetics of polyelectrolyte adsorption onto polystyrene latex particle studied using electrophoresis: Effects of molecular weight and ionic strength

2006 ◽  
Vol 300 (1) ◽  
pp. 69-77 ◽  
Author(s):  
K. Aoki ◽  
Y. Adachi
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Latex Particle ◽  
Polystyrene Latex ◽  
Polyelectrolyte Adsorption ◽  
Kinetics Of

KINETIC EFFECTS OF HIGH MOLECULAR WEIGHT KININOGEN AND ZINC ON CONTACT ACTIVATION

1987 ◽  
Author(s):  
J D Shore ◽  
D E Day ◽  
S T Olson
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
High Molecular Weight ◽  
Proper Function ◽  
Factor Xii ◽  
High Molecular Weight Kininogen ◽  
Contact Activation ◽  
Kinetic Effects ◽  
Activation Rates ◽  
Kinetics Of

Previous work in our laboratory showed that Zn2+ enhanced the rate of kallikrein generation by dextran sulfate (DxSO4) in dialyzed normal plasma, but not in Fitzgerald or Hageman prismas. This could be partially explained by a marked effect of Zn2+ on factor XII autoactivation, and our present work involves zinc effects on other reactions of contact activation. At physiological ionic strength (0.15 μ), the kcat/Km for Xlla activation of prekallikrein (PK) was 0.62 μM™1 s™1 which was increased to 4.35 μM™1 s™1 by the presence of 25μg/ml DxSO4. High molecular weight kininogen (HMK) at 40 nM further increased this to 10.8 μM™1 s™1 , and 5 ¼M Zn2+ had no effect. To determine whether these cofactors promote a surface-dependent activation of PK by XIIa under conditions which weaken the protein-surface interactions, the kinetics were examined at 0.3μ. At this ionic strength, kcat/Km was 0.18 μM™1 s™1 and was unchanged by 25μg/ml DxSO4. This was increased to .805 μM™1 s™1 by 150 nM HMK and further increased 10-fold to 8.35 μM™1 s™1 by 10 μM™1 Zn2+ . Qualitative results were obtained at 0.3 μ for the other reciprocal reaction, XII activation by kallikrein (K). To observe XII activation within 2 hours, both 10 μM Zn2+ and 25 μM HMK were essential, indicating that these cofactors have a very large enhancing effect on the kinetics of this reaction. Chromatography of HMWK on DxSO4-agarose ^ljiowed elution of the protein at 0.42 M NaCl in the absence of Zn2+ ,but at 0.88M in its presence, providing evidence that Zn+ markedly increases the affinity of HMK for DxSO4. Our results are consistent with the increased activation rates observed in the presence of Zn2+ and HMK due to enhanced binding affinity of the reacting proteins to surfaces. This is likely to be essential for proper function of the contact system in blood, where many other proteins compete for surface. Supported by USPHS grant HL-25670

Antithrombin III Binding to Surface Immobilized Heparin and Its Relation to F Xa Inhibition

1987 ◽  
Vol 58 (04) ◽  
pp. 1064-1067 ◽  
Author(s):  
K Kodama ◽  
B Pasche ◽  
P Olsson ◽  
J Swedenborg ◽  
L Adolfsson ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Surface Coating ◽  
Antithrombin Iii ◽  
Lower Class ◽  
Biologically Active ◽  
High Affinity ◽  
Heparin Coating ◽  
Continuous Surface ◽  
Approximate Molecular Weight

SummaryThe mode of F Xa inhibition was investigated on a thromboresistant surface with end-point attached partially depoly-merized heparin of an approximate molecular weight of 8000. Affinity chromatography revealed that one fourth of the heparin used in surface coating had high affinity for antithrombin III (AT). The heparin surface adsorbed AT from both human plasma and solutions of purified AT. By increasing the ionic strength in the AT solution the existence of high and low affinity sites could be shown. The uptake of AT was measured and the density of available high and low affinity sites was found to be in the range of 5 HTid 11 pic.omoles/cmf, respectively Thus the estimated density of biologically active high and low ailmity heparm respectively would be 40 and 90 ng/cm2 The heparin coating did not take up or exert F Xa inhibition by itself. With AT adsorbed on both high and low affinity heparin the surface had the capacity to inhibit several consecutive aliquots of F Xa exposed to the surface. When mainly high affinity sites were saturated with AT the inhibition capacity was considerably lower. Tt was demonstrated that the density of AT on both high and low affinity heparin determines the F Xa inhibition capacity whereas the amount of AT on high affinity sites limits the rate of the reaction. This implies that during the inhibition of F Xa there is a continuous surface-diffusion of AT from sites of a lower class to the high affinity sites where the F Xa/AT complex is formed and leaves the surface. The ability of the immobilized heparin to catalyze inhibition of F Xa is likely to be an important component for the thromboresistant properties of a heparin coating with non-compromized AT binding sequences.

Interaction of Plasminogen Activators and Plasminogen with Heparin: Effect of Ionic Strength

1993 ◽  
Vol 70 (05) ◽  
pp. 867-872 ◽  
Author(s):  
Dingeman C Rijken ◽  
Gerard A W de Munk ◽  
Annie F H Jie
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Plasminogen Activator ◽  
Plasminogen Activators ◽  
Fibrinolytic System ◽  
Tissue Type ◽  
Single Chain ◽  
Physiological Conditions ◽  
Amino Terminal ◽  
Type Plasminogen Activator

SummaryIn order to define the possible effects of heparin on the fibrinolytic system under physiological conditions, we studied the interactions of this drug with plasminogen and its activators at various ionic strengths. As reported in recent literature, heparin stimulated the activation of Lys-plasminogen by high molecular weight (HMW) and low molecular weight (LMW) two-chain urokinase-type plasminogen activator (u-PA) and two-chain tissue-type plasminogen activator (t-PA) 10- to 17-fold. Our results showed, however, that this stimulation only occurred at low ionic strength and was negligible at a physiological salt concentration. Direct binding studies were performed using heparin-agarose column chromatography. The interaction between heparin and Lys-plasminogen appeared to be salt sensitive, which explains at least in part why heparin did not stimulate plasminogen activation at 0.15 M NaCl. The binding of u-PA and t-PA to heparinagarose was less salt sensitive. Results were consistent with heparin binding sites on both LMW u-PA and the amino-terminal part of HMW u-PA. Single-chain t-PA bound more avidly than two-chain t-PA. The interactions between heparin and plasminogen activators can occur under physiological conditions and may modulate the fibrinolytic system.

Antiheparin Activity of Human Serum and Platelet Factor 4

1973 ◽  
Vol 30 (01) ◽  
pp. 093-105 ◽  
Author(s):  
C.H.J Sear ◽  
L Poller ◽  
F.R.C Path
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Blood Serum ◽  
Whole Blood ◽  
Platelet Rich Plasma ◽  
Gel Filtration ◽  
Normal Serum ◽  
Platelet Factor ◽  
Mean Values ◽  
Antiheparin Activity

SummaryThe antiheparin activity of normal serum has been studied by comparing the antiheparin activities of sera obtained from normal whole blood, platelet-rich plasma and platelet-’free’ plasma with a purified platelet extract during differential isoelectric precipitation and by gel filtration chromatography.The mean values for the activity of PRP-serum and PFP-serum were 106% (S.D. 11) and 10% (S.D. 3) of untreated whole blood respectively. The activity of whole blood serum, PRP serum and whole blood serum plus platelet extract precipitated under identical physical conditions, i.e. pH 7.0, I =0.008, indicating that the activities of the three samples are probably associated with PF4. PF4 precipitated from human platelet extract at pH 4.0, but this is probably due to the difference in the two biochemical environments investigated, i.e. serum and platelet extract.The gel filtration experiments revealed striking similarities between the major antiheparin activities of serum and platelet extract. At physiological pH and ionic strength both activities were associated with high molecular weight material, but at physiological pH and elevated ionic strength both activities behaved as much smaller entities of molecular weight between 25,000 and 30,000 daltons and it seems very likely that both activities are associated with the same molecule, i.e. PF4.

Study of the Cu(II) removal from aqueous solutions by adsorption on titania

2013 ◽  
Vol 12 (3) ◽  
pp. 239-247
Keyword(s):  
Heavy Metals ◽  
Ionic Strength ◽  
Toxic Metals ◽  
Low Cost ◽  
Lateral Interaction ◽  
Tio2 Surface ◽  
High Toxicity ◽  
Removal Of Heavy Metals ◽  
Solution Parameters ◽  
Kinetics Of

The removal of heavy metals from wastewaters is a matter of paramount importance due to the fact that their high toxicity causes major environmental pollution problems. One of the most efficient, applicable and low cost methods for the removal of toxic metals from aqueous solutions is that of their adsorption on an inorganic adsorbent. In order to achieve high efficiency, it is important to understand the influence of the solution parameters on the extent of the adsorption, as well as the kinetics of the adsorption. In the present work, the adsorption of Cu(II) species onto TiO2 surface was studied. It was found that the adsorption is a rapid process and it is not affected by the value of ionic strength. In addition, it was found that by increasing the pH, the adsorbed amount of Cu2+ ions and the value of the adsorption constant increase, whereas the value of the lateral interaction energy decreases.

Particle Destabilization in Turbulent Pipe Flow

1989 ◽  
Vol 21 (6-7) ◽  
pp. 435-442 ◽  
Author(s):  
B. Döll
Keyword(s):  
Pipe Flow ◽  
Reaction Rate ◽  
Turbulent Pipe Flow ◽  
Cationic Polymers ◽  
Flow Conditions ◽  
Polyelectrolyte Adsorption ◽  
Charge Neutralization ◽  
Silica Suspensions ◽  
Kinetics Of ◽  
Turbulent Flow Conditions

Silica suspensions (pH = 6.8) and three different cationic polymers were used to study the kinetics of charge neutralization by polyelectrolyte adsorption. The experiments were performed in a continuous flow pipe reactor under steady state turbulent flow conditions. The charge neutralization was monitored by electrophoretic mobility (EPM) measurements of the suspended particles as a function of time after polyelectrolyte audition. The results show the dependency of the destabilization reaction rate on flow and polymer characteristics.

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