We presented evidence indicating that the established procedure for purifying delta-aminolaevulinate (ALA) synthase from embryonic-chick liver yielded an enzyme with a partially degraded subunit of molecular weight 51000 [Ades & Harpe (1981) J. Biol. Chem. 256, 9329-9333]. We now report the purification from livers of porphyric embryos of a preparation of ALA synthase which consisted primarily of a 63000-Da polypeptide and a component migrating as a smear of polypeptides with a minimum molecular weight of 52 000. Neither component could be recovered from liver mitochondria of normal embryos, where the amounts of ALA synthase were relatively low. The 52 000-Da component had been established to be the partially degraded subunit of the enzyme. Peptide-mapping analyses indicated that the 63 000- and the 52 000-Da components possessed significant structural homologies, and it was concluded that the 63 000-Da polypeptide represented the mature subunit of ALA synthase.
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Research Article| August 01 1982
Isolation of the mature subunit of δ-aminolaevulinate synthase from embryonic chick liver
Biochem J (1982) 205 (2): 257–263.
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I Z Ades, K G Harpe; Isolation of the mature subunit of δ-aminolaevulinate synthase from embryonic chick liver. Biochem J 1 August 1982; 205 (2): 257–263. doi: https://doi.org/10.1042/bj2050257
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