Fractionation of human plasma proteins by hydrophobic interaction membrane chromatography

✍ Scribed by Raja Ghosh

• Publisher: Elsevier Science
• Year: 2005
• Tongue: English
• Weight: 346 KB
• Volume: 260
• Category: Article
• ISSN: 0376-7388
• DOI: 10.1016/j.memsci.2005.03.024

✦ Synopsis

This paper discusses the fractionation of human plasma proteins HSA and HIgG by hydrophobic interaction membrane chromatography. A type of microporous polyvinylidine fluoride (PVDF) membrane having 0.1 m pore size was identified as being suitable for carrying out this separation. This membrane bound HIgG at 1.5 M ammonium sulphate concentration, a condition at which HSA did not. Based on this selective binding resulting from the selective pressure induced by the high anti-chaotropic salt concentration, these human plasma proteins were fractionated. The HIgG binding capacity of the PVDF membrane examined in this study was 42.8 mg/ml at a feed concentration of 0.45 mg/ml. Separation of simulated HSA/HIgG mixtures were carried out in the pulse and step input modes and the HSA and HIgG fractions thus obtained were analysed for purity using affinity chromatography and SDS-PAGE. HSA and HIgG purities were typically in excess of 97-98%.