Heterogeneity and oxidation status of commercial human albumin preparations in clinical use.
OBJECTIVE
Human serum albumin is indicated for the treatment of shock, acute restoration of blood volume, and in hypoalbuminemia. Conflicting reports are found in the literature for the clinical safety and efficacy of human serum albumin administration to critically ill patients. We sought to analyze various commercially available albumin preparations for common, posttranslational modifications.


METHODS
Analysis of six commercially available albumin preparations for clinical use.


METHODS
Trauma research laboratory.


METHODS
Commercially available human serum albumin preparations and healthy volunteers.


METHODS
Six commercially available human serum albumin preparations were analyzed by high-performance liquid chromatography. The presence of various posttranslational modifications was identified by positive electrospray ionization, time-of-flight mass spectrometry. Three different lots from three preparations were also analyzed to assess variability within lots from the same manufacturer. Also, for the purpose of comparison, human serum albumin was analyzed in the plasma of healthy volunteers.


RESULTS
The six human serum albumin preparations analyzed contained a high percentage (57.2 +/- 3.3%) of bound Cys34 (oxidation of cysteine in position 34 on the human serum albumin molecule) in comparison to the plasma human serum albumin from healthy volunteers (22.9 +/- 4.8%). Lot-to-lot variability in native human serum albumin ranged between 4.8% and 11.2% in three separate commercial albumins. Significant differences existed among the various commercial preparations in other posttranslational modifications of albumin.


CONCLUSIONS
Human serum albumin species with a bound Cys34 account for a large percentage of the composition of human serum albumin preparations used for the treatment of critically ill patients. Also, the variability within lots from the same manufacturer is significant. Consequences of the administration of these oxidized forms of human serum albumin to critically ill patients warrants further investigation.
Swedish Medical Center, Trauma Research Laboratory, Englewood, CO 80113, USA.
David
D
Bar-Or
Raphael
R
Bar-Or
Leonard T
LT
Rael
David K
DK
Gardner
Denetta S
DS
Slone
Michael L
ML
Craun
D002851:Chromatography, High Pressure Liquid; D006801:Humans; D010084:Oxidation-Reduction; D012709:Serum Albumin / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization
D012709:Serum Albumin