On-siteColorimetric Forensic Sensor (II): Quantitative Detection of Toxic S2-Ion in Blood Plasma Using Metal-Ion-modified Silica Powders

2015 ◽  
Vol 36 (10) ◽  
pp. 2506-2510
Author(s):  
Seung-Jin Ryu ◽  
Eric Arifin ◽  
Shin-Woo Ha ◽  
Jin-Kyu Lee
Biomedicines ◽  
2020 ◽  
Vol 8 (5) ◽  
pp. 133
Author(s):  
Sergey Radko ◽  
Konstantin Ptitsyn ◽  
Svetlana Novikova ◽  
Yana Kiseleva ◽  
Alexander Moysa ◽  
...  

Selected reaction monitoring (SRM) is a mass spectrometric technique characterized by the exceptionally high selectivity and sensitivity of protein detection. However, even with this technique, the quantitative detection of low- and ultralow-abundance proteins in blood plasma, which is of great importance for the search and verification of novel protein disease markers, is a challenging task due to the immense dynamic range of protein abundance levels. One approach used to overcome this problem is the immunoaffinity enrichment of target proteins for SRM analysis, employing monoclonal antibodies. Aptamers appear as a promising alternative to antibodies for affinity enrichment. Here, using recombinant protein SMAD4 as a model target added at known concentrations to human blood plasma and SRM as a detection method, we investigated a relationship between the initial amount of the target protein and its amount in the fraction enriched with SMAD4 by an anti-SMAD4 DNA-aptamer immobilized on magnetic beads. It was found that the aptamer-based enrichment provided a 30-fold increase in the sensitivity of SRM detection of SMAD4. These results indicate that the aptamer-based affinity enrichment of target proteins can be successfully employed to improve quantitative detection of low-abundance proteins by SRM in undepleted human blood plasma.


2002 ◽  
Vol 90 (4) ◽  
Author(s):  
N. V. Jarvis ◽  
J. R. Zeevaart ◽  
J. M. Wagener ◽  
W. K. A. Louw ◽  
I. C. Dormehl ◽  
...  

SummaryA water-soluble polymer, polyethyleneimine functionalised with methylene phosphonate groups (PEI-MP) and labelled with


Sign in / Sign up

Export Citation Format

Share Document