Albumin transport analysis of different collected and processed plasma products by electron spin resonance spectroscopy.
BACKGROUND
Changes of albumin conformation flexibility and binding characteristics in plasma products can be determined by electron spin resonance spectroscopy (ESR) with spin probes as reporter molecules.


METHODS
Quality of albumin transport was analyzed in different processed plasma units using a new ESR method which provides estimation of albumin properties by examination of albumin molecular structure changes.


RESULTS
In serum of healthy donors could not be obtained any abnormalities. Transport function of albumin in plasma products can be influenced by various methods of plasma collection, preparation, and filtration. Evident are changes in capacity of fatty acid binding sites and ordering changes of bound substrates. Transport respiratory detoxification efficiency is decreased between 30% and 70% in all FFP compared to control values.


CONCLUSIONS
ESR spectroscopy can be used as a quality test for plasma. The ESR technique has a big potential for determination of conformation changes of macromolecules and as a global tumor marker test for donor screening.
D001692:Biological Transport; D015415:Biomarkers / Q000097:blood; D001781:Blood Component Removal / Q000379:methods / Q000592:standards*; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D018583:Pliability; D011485:Protein Binding; D011487:Protein Conformation; D011786:Quality Control; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology
D015415:Biomarkers; D012709:Serum Albumin