Abstract
The effective isolation of small peptides has been achieved by HPLC with alumina supports and hydrophilic eluents combined with a reversed phase HPLC. Of the four kinds of alumina supports tested, only Spherisorb A5Y showed the high column efficiency and a good reproducibility. Its elution mode appeared to be the same as the open column system, judging from the chromatograms of synthetic phyllolitorin and bradykinin. A mixture of the tryptic fragments of egg white lysozyme was separated by the combination of alumina and ODS columns, with a linear gradient elution of acetonitrile. The peaks which could not be isolated by one column were effectively separated by a second column; this was confirmed by determining their amino acid compositions. Spherisorb A5Y was found by the fluorescent X-ray analysis to be a complexed material of aluminum oxide and titanium oxide.
