Abstract
Chromatography on DEAE (diethylaminoethyl) cellulose and subsequent ultracentrifugation were carried out on commercial preparations of normal human serum albumin stored under various conditions for at least 10 years. One lot of albumin prepared from citrated whole plasma and stored in solution at 5[degree] C showed little difference in chromatographic behavior from fresh albumin. The storage of samples from this lot at 32[degree] C produced large amounts of material that appeared later in the elution patterns and included components with sedimentation coefficients greater than 5.6 S. Regardless of temperature, albumin stored as a 5% protein solution underwent somewhat less change than that stored as a 25% solution and much less than that stored in the dry state. Samples prepared from ultraviolet-irradiated, dried plasma were less stable than those prepared from citrated whole plasma, irrespective of the storage conditions. Three out of four lots stored at 32[degree] C in the dry state, the most deleterious storage condition found in this study, exhibited, in addition to the above changes, a component that did not bind to the DEAE cellulose and consisted of materials with sedimentation coefficients of 10 S or greater.