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Rapid purification of arrowhead proteinase inhibitors by high performance hydrophobic interaction chromatography on a PEG bonded phase column
Author(s) -
Chang JenPing,
Yuan Yun
Publication year - 1987
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.1130020107
Subject(s) - chemistry , chromatography , hydrophilic interaction chromatography , high performance liquid chromatography , ammonium sulfate , phosphate , peg ratio , phosphate buffered saline , chromatography column , cellulose , column chromatography , phase (matter) , hydrophobic effect , salt (chemistry) , biochemistry , organic chemistry , finance , economics
A new hydrophobic interaction HPLC column is used for the rapid purification of proteinase inhibitors isolated from arrowhead. The inhibitors, partially purified by DEAE‐cellulose column chromatography, are resolved into three components with a mobile phase gradient of decreasing salt concentration from 1.1 M ammonium sulfate in 0.01 M phosphate buffer to phosphate buffer alone. This new HPLC column is found to be very useful for rapid, semipreparative purification of hydrophobic protein and sample loading of up to 1.6 mg of inhibitors can be fully resolved on an analytical column.