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Updated: Oct 12, 2026

Preparation of Highly Coupled Rat Heart Mitochondria
Published on: September 23, 2010
The import of carbamoyl-phosphate synthase into mitochondria from foetal rat liver
Abstract:
A putative precursor of carbamoyl-phosphate synthase was isolated from a microsomal wash fraction and purified by high-pressure liquid chromatography. Autolytic degradation and limited proteolysis were used to characterize the putative precursor of carbamoyl-phosphate synthase and to show its similarity to the processed enzyme. The carbamoyl-phosphate synthase precursor underwent a time-dependent and concentration-dependent conversion into a dimeric or polymeric form. When labelled with 125I and incubated with foetal rat liver mitochondria the precursor was bound to the mitochondria and about 30% of the label was imported into the matrix space. This labelling required the presence of ATP and was time-dependent. Mitoplasts also imported the carbamoyl-phosphate synthase precursor. After import of the precursor, increases in carbamoyl-phosphate synthase activity could be demonstrated in foetal rat liver mitochondria.
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