Abstract
That the macroporous anion-exchange resin AG MP-1 can be used with HPLC equipment and common aqueous buffers for the chromatography of proteins is shown. The utility of this system is illustrated by the partial purification and complete resolution of the three protein synthesis elongation factors from each other, starting with a crude extract of Escherichia coli. The factors were purified 10- to 30-fold in a yield of 50 to 90% with a single 60-min chromatographic program of increasing NaCl concentration. Other proteins from various biological sources were purified with similar results. Thus, it appears that AG MP-1 is useful, at least in some applications, for the rapid, reproducible, and economical purification of proteins using HPLC equipment.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 373-377 |
| Number of pages | 5 |
| Journal | Analytical Biochemistry |
| Volume | 142 |
| Issue number | 2 |
| DOIs | |
| State | Published - Nov 1 1984 |
Bibliographical note
Funding Information:’ This research was supported by Grants GM-21359 and GM-26832 from the National Institutes of Health to JWB. The authors of this paper are listed in alphabetical order.