EurA1c: the European HbA1c Trial to Investigate the Performance of HbA1c Assays in 2166 Laboratories across 17 Countries and 24 Manufacturers by Use of the IFCC Model for Quality Targets

Background: A major objective of the IFCC Committee on Education and Use of Biomarkers in Diabetes is to generate awareness and improvement of HbA1c assays through evaluation of the performance by countries and manufacturers. Methods: Fresh whole blood and lyophilized hemolysate specimens manufactured from the same pool were used by 17 external quality assessment organizers to evaluate analytical performance of 2166 laboratories. Results were evaluated per country, per manufacturer, and per manufacturer and country combined according to criteria of the IFCC model for quality targets. Results: At the country level with fresh whole blood specimens, 6 countries met the IFCC criterion, 2 did not, and 2 were borderline. With lyophilized hemolysates, 5 countries met the criterion, 2 did not, and 3 were borderline. At the manufacturer level using fresh whole blood specimens, 13 manufacturers met the criterion, 8 did not, and 3 were borderline. Using lyophilized hemolysates, 7 manufacturers met the criterion, 6 did not, and 3 were borderline. In both country and manufacturer groups, the major contribution to total error derived from between-laboratory variation. There were no substantial differences in performance between groups using fresh whole blood or lyophilized hemolysate samples. Conclusions: The state of the art is that 1 of 20 laboratories does not meet the IFCC criterion, but there are substantial differences between country and between manufacturer groups. Efforts to further improve quality should focus on reducing between-laboratory variation. With some limitations, fresh whole blood and well-defined lyophilized specimens are suitable for purpose

Quantitative measurement of the mechanical properties of human antibodies with sub-10-nm resolution in a liquid environment

The nanomechanical properties of single human immunoglobulin G and M antibodies were measured in a liquid environment using a fast force-volume technique with sub-10-nm spatial resolution. The ultrastructural details of these molecules were resolved in the images. Simultaneously, important physical properties, including elasticity, adhesion, and deformation were measured. The dimensions and adsorption of the immunoglobulin M antibodies onto the substrate indicated that they are highly flexible. The antibodies were characterized by a low elastic stiffness (34 +/- 10 MPa) and high deformability (1.5 +/- 0.5 nm)