A new method of purification has been developed for peptides synthesised by the Merrifield solid phase methodology. N<SUP>PROB*LEM</SUP>-17-Tetrabenzo(a,c,g,i)fluorenylmethoxycarbonyl glycine (Tbfmoc Gly OH) has been prepared, and coupled <i>via</i> its symmetrical anhydride or its HOBt ester to the N-terminus of a peptide at the final stage of the synthesis. The strong affinity of the Tbfmoc group for graphitised carbon (PGC) allows the retention of Tbfmoc-protected peptides on a column packed with this material, whilst incorrectly terminated sequences and other materials are washed away. Following deprotection of the Tbfmoc group under basic conditions, the free peptide can be eluted from the column. This method has been exemplified by the purification of Ubiquitin (53-76) OH and Ubiquitin (35-76) OH. Preliminary results indicate that the technique may be developed into a form of affinity purification suitable for the resolution of racemates using ligand-exchange chromatography (LEC).
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:660943 |
| Date | January 1990 |
| Creators | Raphy, Gilles |
| Publisher | University of Edinburgh |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://hdl.handle.net/1842/14254 |
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