Purification of rat liver mitochondrial δ-aminolaevulinate synthase

Abstract

Mitochondrial δ-aminolaevulinate synthase was purified from drug-induced adult rat liver and identified for the first time as a protein of minimum molecular weight 70,000. The enzyme was also identified in mitochondria by pulse-labelling and immunoprecipitation and shown to have a molecular weight of 70,000. The purified enzyme was degraded by papain to smaller forms of molecular weight about 56,000 with no loss of enzyme activity. In vitro translation experiments suggest that the enzyme is synthesized initially as a larger precursor of molecular weight 76,000. © 1982.