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For subsequent fractionation by anion exchange, size-exclusion fractions were concentrated and injected onto a Mono-Q FPLC column (Amersham Pharmacia) equilibrated with FPLC buffer at 0.1 M NaCl.
After dialysis, purified protein was obtained after anion-exchange, size exclusion on FPLC, and polymyxin B affinity chromatography.
Five ACE inhibitory peptides were purified from the oyster hydrolysate using a multistep chromatographic procedure comprised of ion-exchange, size exclusion, and reversed-phase liquid chromatography.
Five ACE inhibitory peptides were purified and identified from the oyster hydrolysate using ion-exchange, size exclusion, and reversed-phase chromatography.
In some organisms, e.g., Drosophila and perhaps man, distributive pairing (i.e., a psot-exchange, size-dependent pairing) ensures the regular segregation of such homologous univalents.
The buffer of this sample was exchanged with buffer C. The sample was further purified by anion exchange and size exclusion chromatography as described for the kinetic analysis, except that the eluted sample of the size exclusion column was just concentrated for crystallization.
The His-tagged TM0415 enzymes for kinetic analysis were purified by Ni affinity, anion exchange, and size exclusion chromatography.
Purification of the non-tagged TM0415 for crystallization was performed by heat treatment, anion exchange, and size exclusion chromatography.
Purification methods are currently dominated by ion exchange and size exclusion chromatography.
