Novel hydrophobic interaction chromatography matrix for specific isolation and simple elution of immunoglobulins (A, G, and M) from porcine serum

Biorecognition of Escherichia coli K88 adhesin for glycated porcine albumin

“…Albumin fraction (containing mainly albumin and some of immunoglobulins) was isolated by hydrophobic interaction chromatography (HIC) using a highly acetylated Sepharose (HASepharose) according to Ramos-Clamont et al [22]. PSA was purified by pseudo-affinity chromatography using a 5 mL prepacked Affi-Gel Blue column (Agarose-Cibacron Blue F3GA) from BioRad (Hercules, CA, USA).…”

“…Albumin enriched fractions (40 mg) obtained from HA-Sepharose chromatography [22] were applied to Affi-Gel Blue column. Unadsorbed proteins were washed with Buffer A, while those interacting with the matrix eluted with 1.4 M NaCl in Buffer A. SDS-PAGE analysis of eluted fractions showed only a 66 kDa band that corresponded to porcine serum albumin (Fig.…”

Use of mep HyperCel for polishing of human serum albumin

“…There have been a number of reports that hydrophobic interaction chromatography (HIC) offers sufficient selectivity to allow separation of plasma proteins based on differences in the surface hydrophobicity of the proteins [11,12]. This has allowed HIC to be used successfully for the purification of albumin from human plasma [13], human placenta [14] and of recombinant human serum albumin from Pichia pastoris [15].…”

Depletion of highly abundant proteins in blood plasma by hydrophobic interaction chromatography for proteomic analysis

“…The results obtained by HIC were similar to those obtained by ion exchange chromatography. On the other hand, a HIC matrix consisting of highly acetylated agarose has been used for the isolation of immunoglobulin from porcine serum, with a relative success [16].…”