Jan 1, 1975

Alternatives to freeze-drying for the removal of ethanol from plasma proteins. II. Gel filtration of albumin

Vox Sanguinis
A J Dickson, J K Smith


Removal of ethanol from highly concentrated solutions of human albumin (Cohn fraction V) by gel filtration on Sephadex G-25 is hindered by the contraction of the gel in ethanolic solution, by incomplete retardation of ethanol compared with other low MW solutes, and by restricted diffusion of ethanol from the albumin zone. Despite these obstacles, the hourly capacity of such gel filtration columns, for approximately 100-fold reduction of ethanol concentration, may exceed 0.06 kg albumin per litre of column volume. The gel can be used safely at 5 degrees C for several years. The ethanol content of the final product is higher than that achieved by vacuum distillation, and it may be desirable to operate the two techniques sequentially.

Mentioned in this Paper

Restricted Diffusion
Ethanol Measurement
Sephadex G 25
Albumin Human, USP
Contraction (Finding)
Glass (Substance)
Cohn fraction V
Plasma Proteins

About this Paper

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