Publications by authors named "A J Van Raaij"

Objectives: The aim of this study was to assess the feasibility of testing actionable mutations in small amounts of formalin-fixed paraffin-embedded material in multiple genes of the receptor tyrosine kinase pathway and to determine the frequency of these mutations in human papillomavirus (HPV)-positive and HPV-negative oropharyngeal cancer (OPC).

Design: A retrospective pilot study was performed.

Setting: In OPC, no predictive markers for response to epidermal growth factor receptor inhibition are known.

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The BIOMED-2 protocol is widely used for detecting clonality in lymphoproliferative disorders. The protocol requires multiple PCR reactions, which are analyzed by either capillary electrophoresis (GeneScan analysis) or heteroduplex PAGE analysis. We tested a microfluidic chip-based electrophoresis device (Agilent 2100 Bioanalyzer) for the analysis of B-cell clonality using PCR for the three framework subregions (FR) of the Ig heavy chain gene (IGH) and PCR for two rearrangements occurring in the Ig κ chain gene (IGK-VJ and IGK-DE).

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Calf lens fiber membranes and fractions enriched in junction-like structures have been isolated in the absence and presence of EDTA. Their biochemical features have been studied. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and immunoblotting experiments have provided evidence that a distinct group of EDTA-extractable proteins, being one of the main protein components of calf lens fiber membranes and very likely also of junction-like structures, is bound to these membranes via calcium ions.

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An antiserum has been prepared against the EDTA-extractable proteins (EEP) from calf lens fiber membranes. It was shown to be highly specific for EEP. Using this anti-EEP antiserum in (crossed-line) immunoelectrophoresis and (crossed) immunoelectrofocusing experiments, evidence was obtained that all of the EDTA-extractable proteins are immunologically related.

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The eye lens membrane component 'MP34' [Exp. Eye Res. 24 (1977) 413-415] has been resolved into three protein components and in a revised nomenclature designated MP35, MP36.

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