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The fractionation of the plasma proteins human serum albumin (HSA) and human immunoglobulins (HIgG) using the combination of two newly developed techniques, pulsed sample injection technique and carrier phase ultrafiltration (CPUF), is discussed in this paper. The effects of pH and ionic strength on the transmission of a single protein (i.e., either HSA or HIgG) through 100 and 300 kDa MWCO polyethersulfone (PES) membranes were quantified using the pulsed sample injection technique. The experimental results thus obtained suggested that it would be possible to fractionate these proteins by optimizing the solution pH and ionic strength. With 100 and 300 kDa PES membranes, effective separation of HSA and HIgG was achieved by CPUF using suitable conditions, i.e., pH 4.7 and low salt concentration. The fractionation of HSA and HIgG by "reverse selectivity" using 300 kDa membranes was also examined.

Original publication

DOI

10.1021/bp0343716

Type

Journal article

Journal

Biotechnol Prog

Publication Date

07/2004

Volume

20

Pages

1103 - 1112

Keywords

Electrophoresis, Polyacrylamide Gel, Humans, Hydrogen-Ion Concentration, Immunoglobulin G, Osmolar Concentration, Serum Albumin, Ultrafiltration