Immunological studies of propionyl CoA carboxylase in livers and fibroblasts of patients with propionic acidemia.

Abstract

Antiserum prepared against homogeneous pig heart propionyl CoA carboxylase cross-reacted with human propionyl CoA carboxylase, and was used to demonstrate the presence of immunological cross-reacting material in extracts from the livers of three patients and from fibroblasts of four patients with propionic acidemia representing three major propionyl CoA carboxylase-deficient genetic complementation groups, pcc A, pcc C and bio. Since the quantity of cross-reacting material in the propionyl CoA carboxylase-deficient livers and enzyme-deficient fibroblast cell lines was comparable to that in normal tissues while showing less than five percent of the normal enzyme activity, these patients must synthesize normal or near-normal quantities of an enzymatically inactive propionyl CoA carboxylase protein. In addition, no appreciable change in the amount of cross-reacting material was found in the biotin-responsive bio fibroblasts after incubation with supplemental biotin despite a sixteen-fold increase in enzyme activity suggesting that the defect in the bio mutant involves the activation rather than the synthesis of a pre-existing normal apoenzyme.

• Authors: C McKeon, R Z Eanes, R R Fall, D M Tasset, B Wolf
• Journal: Clinica chimica acta; international journal of clinical chemistry (Clin Chim Acta) Vol. 101 Issue 2-3 Pg. 217-33 (Feb 28 1980) ISSN: 0009-8981 [Print] Netherlands
• PMID: 6766827 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Immune Sera
• Propionates
• Ligases
• Carbon-Carbon Ligases
• propionyl CoA carboxylase (ATP-hydrolyzing)

Topics

• Animals
• Carbon-Carbon Ligases
• Cross Reactions
• Fibroblasts (enzymology)
• Humans
• Immune Sera
• Immunodiffusion
• Ligases (analysis, deficiency)
• Lipid Metabolism, Inborn Errors (enzymology)
• Liver (enzymology)
• Myocardium (enzymology)
• Propionates (metabolism)
• Swine