Human Albumin Samples Research Articles

Validation of GF-AAS Method for the Determination of Aluminium Content in Human Albumin Finished Product

Background: Purified human albumin fractionated from plasma has a complex matrix that imposes a lot of interference in quality control testing, particularly for impurities at trace level. In this study, a simple approach has been studied and validated for the quantification of aluminium content using Graphite Furnace Atomic Absorption Spectrometry (GF-AAS). As per international guidelines, the linearity, accuracy, precision, specificity, limit of detection, and quantification have been assessed. Results: The linearity of the analyte response was evaluated over the range of concentrations from 5μg/L to 45 μg/L, and the correlation coefficient obtained was greater than 0.99. The mean recovery obtained for the accuracy ranged from 102.29% to 106.81% at three concentration levels. The specificity/selectivity evaluated for possible interference from other metal ions and relative standard deviation for the high and low content was 10.24% and 6.50%, respectively, which was statistically verified and not significant. Method precision was evaluated for repeatability and intermediate precision, and the relative standard deviation obtained was 1.83% and 4.61%, respectively. The limit of detection and quantification obtained was 1.30 μg/L and 4.10 μg/L, respectively. Conclusion: Results obtained for the method performance show the suitability of the method for aluminium estimation in human albumin samples and should be used to control the limit of aluminium in human albumin blood products.

Synalbumin, its isolation and conservation.

It has been shown previously that those samples of human albumin which, when freshly isolated using an ethanolic solution of hydrochloric acid, were antagonistic towards insulin lost their activity if stored for a period in air. To eliminate the possibility that antagonist was an artefact of the isolation procedure, samples of air-stored albumins were dissolved in water and subjected to re-extraction using an ethanolic solution of hydrochloric acid. Antagonistic activity was not regenerated. The storage characteristics of albumin isolated by trichloroacetic acid were also studied. It was found that samples stored in air for a period before bioassay were devoid of antagonism. This finding provides a possible explanation for the conflicting results obtained in some previous studies on synalbumin.