báo cáo khoa học: "Quantification of specific bindings of biomolecules by magnetorelaxometry"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Quantification of specific bindings of biomolecules by magnetorelaxometry | Journal of Nanobiotechnology BioMed Central Research Quantification of specific bindings of biomolecules by magnetorelaxometry Dietmar Eberbeck 1 Christian Bergemann2 Frank Wiekhorst1 Uwe Steinhoff1 and Lutz Trahms1 Open Access Address 1Physikalisch-Technische Bundesanstalt Abbestrasse 2-12 D-10587 Berlin Germany and 2Chemicell GmbH Eresburgstrasse 22-23 D12103 Berlin Germany Email Dietmar Eberbeck - Christian Bergemann - info@ Frank Wiekhorst - Uwe Steinhoff- LutzTrahms - Corresponding author Published II March 2008 Received 5 July 2007 Journal of Nanobiotechnology 2008 6 4 doi 1477-3155-6-4 Accepted 11 March 2008 This article is available from http content 6 1 4 2008 Eberbeck et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract The binding reaction of the biomolecules streptavidin and anti-biotin antibody both labelled by magnetic nanoparticles MNP to biotin coated on agarose beads was quantified by magnetorelaxometry MRX . Highly sensitive SQUID-based MRX revealed the immobilization of the MNP caused by the biotin-streptavidin coupling. We found that about 85 of streptavidin-functionalised MNP bound specifically to biotin-agarose beads. On the other hand only 20 of antibiotin-antibody functionalised MNP were specifically bound. Variation of the suspension medium revealed in comparison to phosphate buffer with bovine serum albumin a slight change of the binding behaviour in human serum probably due to the presence of functioning non heated serum proteins. Furthermore in human serum an additional non-specific binding occurs being independent from the serum protein .

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