Development and validation of a quantitative wipe sampling method to determine platinum contamination from antineoplastic drugs on surfaces in workplaces at Swedish hospitals.

Introduction: Antineoplastic drugs (ADs) are frequently used pharmaceuticals in the healthcare, and healthcare workers can be occupationally exposed to ADs. Monitoring of surface contamination is a common way to assess occupational exposure to ADs. The objective was to develop and validate a sensitive and quantitative monitoring method to determine surface contaminations of Pt as a marker for Pt-containing ADs.

Investigating thermally induced aggregation of Somatropin- new insights using orthogonal techniques.

Three orthogonal techniques were used to provide new insights into thermally induced aggregation of the therapeutic protein Somatropin at pH 5.8 and 7.0.

Investigation of native and aggregated therapeutic proteins in human plasma with asymmetrical flow field-flow fractionation and mass spectrometry.

Physiochemical degradation of therapeutic proteins in vivo during plasma circulation after administration can have a detrimental effect on their efficacy and safety profile. During drug product development, in vivo animal studies are necessary to explore in vivo protein behaviour. However, these studies are very demanding and expensive, and the industry is working to decrease the number of in vivo studies.

Revisiting the dynamics of proteins during milk powder hydration using asymmetric flow field-flow fractionation (AF4).

The dynamics of β-casein and casein micelles in the reconstitution of skim milk were revisited in this study. β-casein migrates into casein micelles upon an increase in temperatures due to an increase in the hydrophobic effect and lower calcium-phosphate cluster solubility. This process can be reversed upon cooling.

Investigating the effect of powder manufacturing and reconstitution on casein micelles using asymmetric flow field-flow fractionation (AF4) and transmission electron microscopy.

Milk powders are commonly used for a variety of food products in which among others the milk proteins add to the properties of the products. Processing of milk can, depending on the processing parameters, change the size and structure of the proteins. These changes can be difficult to measure due to the polydispersity of milk components, which makes it a challenge to obtain direct information about the individual proteins.

Asymmetric flow field-flow fractionation coupled to surface plasmon resonance detection for analysis of therapeutic proteins in blood serum.

Coupling of surface plasmon resonance (SPR) detection to asymmetric flow field-flow fractionation (AF4) offers the possibility to study active fractions of bio-separations on real samples, such as serum and saliva, including the assessment of activity of possibly aggregated species. The coupling of SPR with AF4 requires the possibility to select fractions from a fractogram and redirect them to the SPR. The combination of SPR with chromatography-like methods also requires a mechanism for regeneration of the receptor immobilised onto the SPR sensor surface.

Proteins and antibodies in serum, plasma, and whole blood-size characterization using asymmetrical flow field-flow fractionation (AF4).

The analysis of aggregates of therapeutic proteins is crucial in order to ensure efficacy and patient safety. Typically, the analysis is performed in the finished formulation to ensure that aggregates are not present. An important question is, however, what happens to therapeutic proteins, with regard to oligomerization and aggregation, after they have been administrated (i.

Size separations of starch of different botanical origin studied by asymmetrical-flow field-flow fractionation and multiangle light scattering.

Asymmetrical-flow field-flow fractionation combined with multiangle light scattering and refractive index detection has been revealed to be a powerful tool for starch characterization. It is based on size separation according to the hydrodynamic diameter of the starch components. Starch from a wide range of different botanical sources were studied, including normal starch and high-amylose and high-amylopectin starch.

Asymmetrical flow field-flow fractionation coupled with multi-angle light scattering and refractive index detections for characterization of ultra-high molar mass poly(acrylamide) flocculants.

The molar mass distributions of ultra-high molar mass polyacrylamide-based flocculants were measured using asymmetrical flow field-flow fractionation (AFFFF) coupled with multi-angle light scattering and refractive index detectors. The mass load onto the separation channel was found to be critical in obtaining a good size separation. The detailed investigation with ultra-high molar mass polyacrylamides found that the injected amount should be View Article and Find Full Text PDF

Competitive adsorption of a polydisperse polymer during emulsification: experiments and modeling.

In this paper we study the selective adsorption of a high molar mass polymer, OSA-starch, at the cyclohexane/water interface during emulsification. This was made possible through the use of AsFlFFF-MALS-RI which enables us to characterize the size and molar mass of polydisperse ultrahigh molar mass polymers. The results show that the high molar mass components in the molar mass distribution of the polymer were selectively adsorbed.

Programmed cross flow asymmetrical flow field-flow fractionation for the size separation of pullulans and hydroxypropyl cellulose.

Different functions for the programming of the cross flow in asymmetrical flow field-flow fractionation were studied with the aim to find the flow conditions most suitable for the molar mass distribution analysis of high molecular weight polysaccharides. A mixture of four differently sized pullulans covering the molar mass range 5.8 x 10(3)-1.

Mechanical degradation and changes in conformation of hydrophobically modified starch.

In this paper, we study the mechanical degradation and changes in conformation of a branched ultrahigh molar mass biomacromolecule, hydrophobically modified starch, as caused by high-pressure homogenization. The characterization was performed with asymmetrical flow field-flow fractionation (AsFlFFF) with multiangle light scattering (MALS) and refractive index detection. The starch which had been chemically modified with octenyl succinate anhydride (OSA) proved to be very large and polydisperse.

Size characterization of green fluorescent protein inclusion bodies in E. coli using asymmetrical flow field-flow fractionation-multi-angle light scattering.

The goal of this study was to investigate the applicability of asymmetrical flow field-flow fractionation-multi-angle light scattering (AsFlFFF-MALS) for size analysis of green fluorescent protein inclusion bodies (GFPIBs). The size distributions of GFPIBs prepared by various culture conditions were determined. For GFPIBs prepared at 37 degrees C the peak maximum hydrodynamic diameter (d(H)) first increased and then decreased with the increase of the induction times in the presence of 0.