Novel use of an iodo-myristyl-CoA analog identifies a semialdehyde dehydrogenase in bovine liver.

We describe here the identification, purification, and characterization of a semialdehyde dehydrogenaae with a novel fatty acid binding function. The coenzyme A derivative of an 125 I-labeled long chain saturated fatty acid (13-iodo-tridecanoate) was used to tag proteina which bind myristoyl-CoA. A prominent 17 kDa band was identified, which was isolated from bovine liver by a high salt extraction followed by ammonium sulfate precipitation. Sequential chromatographic separation using phenyl-Sepharose, hydroxyapatite, DEAE-Sepharose, Mono Q, and Fast Flow S resins resulted in a purified protein that migrated as a single band of 57 kDa on denaturing gels