Improved separation of biologically active substances on some composite sorbents

Demin, A. A.; Melenevsky, A. T.; Papukova, K. P.; Samsonov, G. V.

doi:10.1016/s0014-3057(00)00073-2

Cited by 2 publications

(2 citation statements)

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“…This is evident in most biological fluids. As a result, protein adsorption may, and in most cases does, play a substantial role in determining the overall efficiencies of certain biological interactions/ processes [37,38]. To this end, we have previously examined the surface coverage of BSA on cotton fibers based on scanning electron microscopy images [39].…”

Section: Modeling Albumin Adsorption On Cottonmentioning

confidence: 99%

“…Although, the kinetics of protein adsorption at the solid/liquid interface have been investigated [35,36], a concise means of measuring protein adsorption kinetics has remained elusive due to the brief time scale of protein binding. Nonetheless, it is important to understand protein adsorption better since it plays a substantial role in determining the overall efficiencies of certain biological interactions/ processes [37,38].…”

Section: Modeling Albumin Adsorption On Cottonmentioning

confidence: 99%

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Chromatographic and Traditional Albumin Isotherms on Cellulose: A Model for Wound Protein Adsorption on Modified Cotton

Edwards¹,

Castro

Condon³

et al. 2011

J Biomater Appl

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Albumin is the most abundant protein found in healing wounds. Traditional and chromatographic protein isotherms of albumin binding on modified cotton fibers are useful in understanding albumin binding to cellulose wound dressings. An important consideration in the design of cellulosic wound dressings is adsorption and accumulation of proteins like albumin at the solid-liquid interface of the biological fluid and wound dressing fiber. To better understand the effect of fiber charge and molecular modifications in cellulose-containing fibers on the binding of serum albumin as observed in protease sequestrant dressings, albumin binding to modified cotton fibers was compared with traditional and chromatographic isotherms. Modified cotton including carboxymethylated, citrate-crosslinked, dialdehyde and phosphorylated cotton, which sequester elastase and collagenase, were compared for their albumin binding isotherms. Albumin isotherms on citrate-cellulose, cross-linked cotton demonstrated a two-fold increased binding affinity over untreated cotton. A comparison of albumin binding between traditional, solution isotherms and chromatographic isotherms on modified cellulose yielded similar equilibrium constants. Application of the binding affinity of albumin obtained in the in vitro protein isotherm to the in vivo wound dressing uptake of the protein is discussed. The chromatographic approach to assessment of albumin isotherms on modified cellulose offers a more rapid approach to evaluating protein binding on modified cellulose over traditional solution approaches.

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Section: Modeling Albumin Adsorption On Cottonmentioning

confidence: 99%