Interactions of human hemoglobin with high‐molecular‐weight dextran sulfate and diethylaminoethyl dextran

Nguyen, Trong Q.

doi:10.1002/macp.1986.021871106

Cited by 22 publications

(17 citation statements)

References 10 publications

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“…These interactions are modulated by such variables as pH and ionic strength, and may result in soluble complexes, 1,2 complex coacervation, [3][4][5][6] or the formation of amorphous precipitates. [7][8][9] Protein-polyelectrolyte complexation can change the activity of catalytic proteins (enzymes), 10 -12 alter ligand binding to transport proteins, 1,7 and stabilize biological activity against temperature change.…”

Section: Introductionmentioning

confidence: 99%

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Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes

et al. 1999

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Quasi-elastic light scattering (QELS), electrophoretic light scattering (ELS), CD spectroscopy, and azide binding titrations were used to study the complexation at pH 6.8 between ferrihemoglobin and three polyelectrolytes that varied in charge density and sign. Both QELS and ELS show that the structure of the soluble complex formed between ferrihemoglobin and poly(diallyldimethylammonium chloride) [PDADMAC] varies with protein concentration. At fixed 1.0 mg/mL polyelectrolyte concentration, protein addition increases complex size and decreases complex mobility in a tightly correlated manner. At 1.0 mg/mL or greater protein concentration, a stable complex is formed between one polyelectrolyte chain and many protein molecules (i.e., an intrapolymer complex) with apparent diameter approximately 2.5 times that of the protein-free polyelectrolyte. Under conditions of excess polyelectrolyte, each of the three ferrihemoglobin-polyelectrolyte solutions exhibits a single diffusion mode in QELS, which indicates that all protein molecules are complexed. CD spectra suggest little or no structural disruption of ferrihemoglobin upon complexation. Azide binding to the ferrihemoglobin-poly(2-acrylamide-2-methylpropanesulfonate)

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Section: Introductionmentioning

confidence: 99%

“…7 Nguyen found a linear decrease in the amount of hemoglobin permeating through the membrane with increasing amount of polyelectrolyte. This linear change in the ultrafiltration indicates an intrapolymer structure for the complex.…”

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confidence: 98%

Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes

et al. 1999

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“…13,[22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39] Interaction of polyelectrolytes with proteins in aqueous solutions is found to be sensitive to pH and ionic strength, as well as be dependent on isoelectric points of proteins. 14,37,40 Polymer-protein complexes form as a result of the electrostatic interaction of polyion chains with the oppositely charged groups of the protein molecules. Binding mode of PEs to proteins is assumed to be dependent on the ratio of components and may result in the formation of soluble polycomplexes, [14][15][16]24 complex coacervation, [25][26][27] or amorphous precipitates.…”

Section: Introductionmentioning

confidence: 99%

“…Soluble polymer–protein complexes were studied by a wide range of methods, which are well known in colloid and polymer chemistry 13, 22–39. Interaction of polyelectrolytes with proteins in aqueous solutions is found to be sensitive to pH and ionic strength, as well as be dependent on isoelectric points of proteins 14, 37, 40. Polymer–protein complexes form as a result of the electrostatic interaction of polyion chains with the oppositely charged groups of the protein molecules.…”

Section: Introductionmentioning

confidence: 99%

High performance liquid chromatography study of water‐soluble complexes and covalent conjugates of polyacrylic acid with bovine serum albumin

Akkiliç

Mustafaeva

Mustafaev

2007

J of Applied Polymer Sci

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Polycomplex formation of bovine serum albumin (BSA) and polyacrylic acid (PAA) was studied by pH titration, fluorescence, and HPLC methods in water solutions. It was shown that the complex formation and the solubility (phase state) of the polycomplexes depended on pH of the solutions and ratio of the components. The stability of PAA-BSA complexes was negligibly weak when pH ¼ 6.0-7.0 [pH > pI (isoelectric pH)]. Stable water-soluble polycomplexes formed at pH ¼ pI (pH 5.0) in a wide range of n BSA /n PAA ratios (0.05-50) and coexisted with free protein molecules at the higher ratios of components. Existence of water-soluble and insoluble PAA-BSA complexes has been observed at pH 4.5. The soluble to insoluble state transition of polycomplexes has been confirmed and binding mode of polyelectrolytes to proteins was assumed dependent on the ratio of components as a result of formation of soluble polycomplexes, complex coacervation, or amorphous precipitates. Soluble complexes were formed as fully homogenized mixtures. Fraction composition of the mixtures and insoluble complexes depended on the protein/polymer ratio and over the critical protein/polymer ratio, the soluble polycomplexes coexisted with free BSA molecules. On the other hand, the comparision of covalent conjugate formation and complexation of PAA with BSA has been revealed.

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“…In addition to protein separation, the use of the protein-polyelectrolyte complex as an enzyme carrier has been of interest, leading to studies of en-The study of protein-polyelectrolyte complexes has been an interesting subject [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] for more than four zyme activity in complexes. For example, Morawetz and co-workers 16 studied the tryptic digestion of decades, in part because of the practical uses of complexation in protein separation.…”

Section: Introductionmentioning

confidence: 99%

Complexation of trypsin and alcohol dehydrogenase with poly(diallyldimethylammonium chloride)

et al. 1997

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Complexation of alcohol dehydrogenase (ADH) and trypsin with poly(diallyldimethyl‐ammonium chloride) (PDADMAC) in dilute electrolyte solution was studied by turbidimetric titration, quasi‐elastic light scattering (QELS), and electrophoretic light scattering (ELS). Both QELS and turbidimetric titration show that PDADMAC forms complexes with ADH and trypsin in 0.01M NaCl solution at pH ≥ 6.8 and pH ≥ 9.2, respectively. These complexes take the form of stable coacervates in 0.01M, pH 11.0, phosphate buffer solution. QELS shows sizes of 400 and 315 nm for the coacervates of ADH‐PDMDAAC and trypsin‐PDMDAAC, respectively, while ELS reveals that these coacervates carry a net positive charge. Activity measurements show that both ADH and trypsin are enzymatically active in their coacervated states. Complexation of trypsin and PDADMAC was also studied by fluorescence in 0.01M, pH 11.0, phosphate buffer, and the protein emission was found to be quenched by complexation. The fluorescence quenching data show that trypsin retains its three‐dimensional structure in the complex. These and other results are consistent with the quenching of the two tryptophans on the protein surface, but not the interior ones.© 1997 John Wiley & Sons, Inc.

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Interactions of human hemoglobin with high‐molecular‐weight dextran sulfate and diethylaminoethyl dextran

Cited by 22 publications

References 10 publications

Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes

Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes

High performance liquid chromatography study of water‐soluble complexes and covalent conjugates of polyacrylic acid with bovine serum albumin

Complexation of trypsin and alcohol dehydrogenase with poly(diallyldimethylammonium chloride)

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