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- W1972684192 endingPage "243" @default.
- W1972684192 startingPage "223" @default.
- W1972684192 abstract "Biological membranes have as a major function the compartmentation of biological processes in cells and organelles. They consist of a bilayer of phospholipid molecules in which proteins are embedded. These integral membrane proteins, which cross the bilayer once or several times, generally have a higher than average hydrophobicity and tend to aggregate. Detergents are needed to remove integral membrane proteins from the lipid bilayer and they have to be present during further chromatographic purification. Predominantly, four modes of HPLC have been used alone or in combination for the puridication of integral membrane proteins. These are based on differences of proteins in size (size-exclusion chromatography, SEC), electrostatic interaction (ion-exchange chromatography, IEC), bioaffinity (bioaffinity chromatography, BAC) and hydrophobic interaction (reversed-phase chromatography, RPC, and hydrophobic-interaction chromatography, HIC). SEC, IEC, BAC and HIC are used under relatively mild conditions, and buffer systems generally contain a non-ionic detergent. RPC generally has a denaturing effect on the protein and should preferably be used for the purification of integral membrane proteins smaller than 50 kD." @default.
- W1972684192 created "2016-06-24" @default.
- W1972684192 creator A5016189502 @default.
- W1972684192 creator A5060432755 @default.
- W1972684192 creator A5067720024 @default.
- W1972684192 date "1987-07-01" @default.
- W1972684192 modified "2023-09-30" @default.
- W1972684192 title "Column liquid chromatography of integral membrane proteins" @default.
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