Use of a selective inhibitor of liver carnitine palmitoyltransferase I (CPT I) allows quantification of its contribution to total CPT I activity in rat heart. Evidence that the dominant cardiac CPT I isoform is identical to the skeletal muscle enzyme-Reference-Cited by-同舟云学术

Use of a selective inhibitor of liver carnitine palmitoyltransferase I (CPT I) allows quantification of its contribution to total CPT I activity in rat heart. Evidence that the dominant cardiac CPT I isoform is identical to the skeletal muscle enzyme

Published:1994-10 Issue:42 Volume:269 Page:26443-26448
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Weis B C,Cowan A T,Brown N,Foster D W,McGarry J D

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference20 articles.

1. Regulation of ketogenesis and the renaissance of carnitine palmitoyltransferase

2. Observations on the affinity for carnitine, and malonyl-CoA sensitivity, of carnitine palmitoyltransferase I in animal and human tissues. Demonstration of the presence of malonyl-CoA in non-hepatic tissues of the rat

3. Inter-tissue and inter-species characteristics of the mitochondrial carnitine palmitoyltransferase enzyme system.

4. Carnitine palmitoyltransferase and carnitine octanoyltransferase activities in liver, kidney cortex, adipocyte, lactating mammary gland, skeletal muscle and heart

5. Rat heart expresses two forms of mitochondrial carnitine palmitoyltransferase I. The minor component is identical to the liver enzyme.

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