Toggle Main Menu Toggle Search

Open Access padlockePrints

Carnitine palmitoyltransferases in pea leaf chloroplasts: partial purification, location, and properties

Lookup NU author(s): Dr Christine Masterson, Dr Cliff Wood


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Carnitine palmitoyltransferase (EC, an enzyme that catalyses the reversible transfer of activated long-chain acyl groups between CoASH and L-carnitine, has been confirmed in pea leaf chloroplasts. This enzyme is bound to the chloroplast inner envelope membrane and has two isoforms, one bound to the outside (cytosol side) of the inner envelope and one bound to the inside (stromal side) of the inner envelope. Malonyl CoA inhibited the activity of the outer carnitine palmitoyltransferase, while stimulating the activity of the inner isoform and may be a regulator of these enzymes in vivo. Carnitine palmitoyltransferase was solubilized from the chloroplast envelope by detergent treatment and the two isoforms separated by Q-Sepharose anion exchange chromatography. Both proteins were immunochemically observed by probing Western blots of sodium dodecyl sulfate - polyacrylamide gel electrophoresis gels using an anti-beef heart mitochondrial carnitine palmitoyltransferase polyclonal antibody. The monomeric molecular mass of the protein recognized by this antibody was approximately 20 kDa. This 20-kDa protein also bound 3H-carnitine. Both isoforms had broad acyl CoA substrate specificities, but showed increased activity with desaturated long-chain acyl CoAs, exhibiting a preference for linolenoyl CoA. A role for carnitine palmitoyltransferase in the shuttling of fatty acids across the chloroplast envelope is suggested.

Publication metadata

Author(s): Masterson C; Wood C

Publication type: Article

Publication status: Published

Journal: Canadian Journal of Botany

Year: 2000

Volume: 78

Issue: 3

Pages: 328-335

Print publication date: 01/01/2000

ISSN (print): 0008-4026

ISSN (electronic): 1916-2804

Publisher: N R C Research Press


DOI: 10.1139/b00-008


Altmetrics provided by Altmetric