Abstract
Two closely eluting hydrophobic peptides, microcystin-LW and -LF had proved in the past to be particularly difficult to purify by reversed-phase HPLC. Initial extraction by reversed-phase flash chromatography provided a good method of concentrating microcystins and also partially purifying them, although the separation of closely eluting variants was not possible. The use of normal-phase flash chromatography after initial reversed-phase extraction was found to be a suitable method for achieving high purity and gave a good yield of both microcystins. However, a final reversed-phase flash step was necessary to eliminate trace contaminants. The method described provides a simple three step flash chromatography extraction and purification eliminating the need to use preparative HPLC.
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