retention order was para, meta, and ortho, as observed with the other systems. However, the meta and ortho isomers were usually very close so that they were eluted as one peak.
CONCLUSIONSThe permanently bound peptide can make an interesting stationary phase. It has a pronounced effect on the elution characteristics of the several classes of compounds which we discussed above. The fact that water was used as the mobile phase in all the studies should be emphasized. The effect of other solvents is being investigated. The poly-Gly peptide can be used in separation of amino acids and para isomers from ortho and meta of some classes of solutes. The fact that the retention behavior was the same on all three support-peptide phase systems seems to demonstrate that the peptide had the major role in the separation. In this connection, it would be of major importance to investigate the effect of the peptide chain length and, perhaps more important, the relative amount of peptide per unit weight of the support on the retention behavior and mechanism. In addition, it seems that the whole peptide chain takes a direct part in the partitioning mechanism and not the terminal group only. This indicates that other polypeptides having different amino acid subunits can be tailored to different separations. These aspects of the peptide phases are now under study.Finally, by using amino acids having asymmetric centers as bound phase, and using, if needed, the recycling techniques recently described by Little (18), separation of d and l amino acids and peptides can be attempted. This is also currently under investigation.
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