Abstract
A method for partial purification of an enzyme system from greening wheat leaves which converts 14C-labeled glutamate to δ-aminolevulinic acid is described. The purification entails the successive use of anion and cation exchange, followed by moleculr sieving. The enzyme system is unstable in crude form, but the stability is markedly increased after column chromatography on CM-cellulose. The pH profile and the cofactor requirements suggest that at least two enzymes are involved.
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