Binding of Bovine Serum Albumin to Heparin Determined by Turbidimetric Titration and Frontal Analysis Continuous Capillary Electrophoresis

Hattori, Toshiaki; Kimura, Kozue; Seyrek, Emek; Dubin, Paul L.

doi:10.1006/abio.2001.5129

Cited by 103 publications

(107 citation statements)

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“…The mole fraction of AMPS units in the copolymer was determined by the ratio between the chemical shifts for C=O of AA units (around 181 ppm) and for C=O of AMPS units (around 178 ppm) according to literature data [11]. The copolymer composition determined by 13 C NMR spectroscopy was in very good agreement with the data obtained by elemental analysis.…”

Section: Resultssupporting

confidence: 52%

“…It is known that PAMPS forms a complex with bovine serum albumin and the binding constant with the protein is very close or nearly identical to that of heparin [13]. It was of interest to evaluate the anticoagulant activity of the copolymers P(AMPS n -co-AA n' ) (2) and to compare it with the effect of PAMPS (3) and PAA (4) Copolymer composition was determined using two independent methods: elemental analysis (sulfur content) and 13 C NMR spectroscopy.…”

Section: Resultsmentioning

confidence: 99%

“…13 C NMR spectra of copolymers were taken on a Bruker MSL 300 spectrometer operating at 75.5 MHz and 300 K in D 2 O, using tetramethylsilane as a reference.…”

Section: Methods For (Co)polymer Characterisationmentioning

confidence: 99%

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Copolymers of 2-acryloylamido-2-methylpropanesulfonic acid and acrylic acid with anticoagulant activity

et al. 2003

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Copolymers of 2-acryloylamido-2-methylpropanesulfonic acid (AMPS) and acrylic acid (AA), as well as the corresponding homopolymers PAMPS and PAA, were studied in vitro on human pool plasma for their anticoagulant activity. The values of the haemostatic parameters -prothrombin time, activated partial thromboplastin time and thrombin time -depend on the composition and the concentration of the (co)polymers. Reptilase time remains unchanged on adding the (co)polymers. A broad concentration range from 16 µg/ml to 3 mg/ml was studied. The copolymers possess anticoagulant activity, which is higher at higher content of AMPS units. It was found that, at certain concentrations, the haemostatic parameters of PAMPS are close to that of heparin. PAA has the lowest anticoagulant activity.

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Section: Resultssupporting

confidence: 52%

Section: Resultsmentioning

confidence: 99%

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Copolymers of 2-acryloylamido-2-methylpropanesulfonic acid and acrylic acid with anticoagulant activity

et al. 2003

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“…The optimal linear arrangements of polyelectrolyte charges are those that maximize attraction with the positive protein domain ("patch") yet minimize repulsion with the surrounding negative protein domain. DMF25, in particular, contains AMPS runs long enough 29 to bind the positive protein domain, and these sequences statistically are readily bracketed by runs of AAm that minimize repulsion from the negative protein domain.…”

Section: Resultsmentioning

confidence: 99%

Effects of Polyelectrolyte Chain Stiffness, Charge Mobility, and Charge Sequences on Binding to Proteins and Micelles

et al. 2006

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The binding affinities of polyanions for bovine serum albumin in NaCl solutions from I ) 0.01-0.6 M, were evaluated on the basis of the pH at the point of incipient binding, converting each such pH c value into a critical protein charge Z c . Analogous values of critical charge for mixed micelles were obtained as the cationic surfactant mole fraction Y c . The data were well fitted as Y c or Z c ) KI a , and values of K and a were considered as a function of normalized polymer charge densities (τ), charge mobility, and chain stiffness. Binding increased with chain flexibility and charge mobility, as expected from simulations and theory. Complex effects of τ were related to intrapolyanion repulsions within micelle-bound loops (seen in the simulations) or negative protein domainpolyanion repulsions. The linearity of Z c with I at I < 0.3 M was explained by using protein electrostatic images, showing that Z c at I < 0.3 M depends on a single positive "patch"; the appearance of multiple positive domains I > 0.3 M (lower pH c ) disrupts this simple behavior.

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“…The above models represent cases in which the binding sites do not interact with each other. Hattori et al [27,28] [29]. This model concerns homogeneous lattices:…”

Section: Fundamentalsmentioning

confidence: 99%

Recent advances in the study of biomolecular interactions by capillary electrophoresis

Ding

et al. 2004

Electrophoresis

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Recent advances in the study of biomolecular interactions by capillary electrophoresisCapillary electrophoresis (CE) has been abundantly used in the study of molecular interactions owing to such advantages as short analysis time, low sample size requirement, high separation efficiency, and flexible applications. The focus of this paper is to review recent studies and advances (mainly from 1998 to now) in biomolecular interactions using CE. Five CE modes: zone migration CE, affinity CE, frontal analysis (FA), Hummel-Dreyer (HD) and vacancy peak (VP) are cited and compared. Quantitative aspects of the thermodynamics and kinetics of biomolecular interaction are reviewed. Several biomolecular binding systems, including protein-protein (polypeptide), protein-DNA (RNA), protein(polypeptide)-carbohydrate, protein-small molecule, DNAsmall molecule, small molecule-small molecule, have been well characterized by CE. CE is shown to be a powerful tool for the determination of the binding parameters of various bioaffinity interactions.

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Binding of Bovine Serum Albumin to Heparin Determined by Turbidimetric Titration and Frontal Analysis Continuous Capillary Electrophoresis

Cited by 103 publications

References 50 publications

Copolymers of 2-acryloylamido-2-methylpropanesulfonic acid and acrylic acid with anticoagulant activity

Copolymers of 2-acryloylamido-2-methylpropanesulfonic acid and acrylic acid with anticoagulant activity

Effects of Polyelectrolyte Chain Stiffness, Charge Mobility, and Charge Sequences on Binding to Proteins and Micelles

Recent advances in the study of biomolecular interactions by capillary electrophoresis

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