Abstract
Properties and Purification of Mitochondrial Propionyl Carboxylase
Highlights
Material and Methods-Coenzyme A, adenosine triphosphate (ATP), and AMP were purchased from Pabst Laboratories
The observation that avidin markedly inhibits propionyl carboxylase activity (Fig. 4) implicates biotin as an essential prosthetic group on this enzyme. The fact that this inhibition could be prevented by prior treatment of avidin with excess biotin indicates that the action of avidin on the carboxylase is probably biotin-specific
Propionyl carboxylase has been partially purified from bovine liver mitochondria and its properties studied
Summary
20 57.0 a Enzyme activity determined with the use of the 040~ fixation propionyl carboxylase assay described in the text. By the use of the 0402 fixation assay described and stored at -20” after removal of ether under reduced pressure Under these conditions, the acetone powder retained its original enzymatic activity for several months. The supernatant was brought to 55% saturation with saturated ammonium sulfate, and after 30 minutes, centrifuged This precipitate was redissolved in 100 ml of 0.0025 M Tris, pH 7.0. Since acetone powder extracts contain several enzymatic activities (ATPase, PPiase, and adenylate kinase) which interfere r Ammonium sulfate was saturated at room temperature and neutralized with NH,OH so that when diluted with 4 volumes of water the pH was 7.5. CoA was analyzed gas chromatographically and found to be free of other low molecular weight aliphatic anhydrides including acetic and propionic anhydrides
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