Abstract
A 15-fold purified preparation from biotin-deficient chicken liver mitochondria catalyzed propionyl-CoA holocarboxylase (PCHC) synthesis in the presence of ATP and d-biotin. UTP effectively replaced ATP in the reaction mixture; with CTP, GTP, or ITP, less than 50% of control activities was observed. Both AMP and ADP inhibited PCHC synthesis. A cytosolic preparation obtained from the same tissue stimulated PCHC synthesis.

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