Identification of the Product of Heme Degradation Catalyzed by the Heme Oxygenase System as Biliverdin IXα by Reversed-Phase High-Performance Liquid Chromatography1

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Abstract
Biliverdins formed from heme by a microsomal preparation and a reconstituted heme oxygenase system were each converted to their dimethyl esters and analyzed for isomeric composition by reversed-phase high-performance liquid chromatography, using a column of μBondapak C18 (Waters Associates); on this column, the dimethyl esters of four biliverdin IX isomers, that is IXα, IXβ, IXγ, and IXδ, have been shown to be eluted separately in the order IXα, IXβ, IXδ, and IXγ, when developed with methanol/water. The analysis indicated that the enzymatically formed biliverdins were exclusively IXα; the elution profile exhibited no other significant elution peak due to other biliverdin isomers. It was concluded that heme ring specifically at the α-methene bridge to yield biliverdin IXα.