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Vitamin A metabolism in chick liver: some properties of the cytosolic lipid–protein aggregate

Published online by Cambridge University Press:  09 March 2007

D. Sklan  and
Orna Halevy
D. Sklan
Affiliation:
Faculty of Agriculture, Hebrew University, Rehovot 76–100, Israel
Orna Halevy
Affiliation:
Faculty of Agriculture, Hebrew University, Rehovot 76–100, Israel
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Abstract

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1. Incubation of hepatic microsomes with retinol resulted in formation of retinyl esters and glucuronides. The presence of the cytosolic lipid-protein aggregate (LPA) in the system in addition induced release of holoretinol-binding protein from the microsomes. The extent of these reactions was influenced by the addition of coenzyme A and ATP, or uridine diphosphate glucuronic acid.

2. Incubation of hepatic microsomes containing labelled retinyl esters with the LPA resulted in the appearance of the labelled retinyl esters in the LPA.

3. Small amounts of retinoic acid were formed on incubation of retinol with microsomes (approximately 1% of added retinol); this was found to be associated with a protein of approximately 14500 molecular weight, and less than 10% was associated with the LPA. This is in contrast to retinol, which was found to be almost completely associated with the LPA.

4. The cytosolic LPA was associated both with carotene-cleavage activity and alcohol dehydrogenase (NAD(P)+) (EC 1. 1. 1. 71) activity.

5. These findings lend some support to the concept of a specific role for hepatic LPA.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 52 , Issue 1 , July 1984 , pp. 107 - 114
Copyright
Copyright © The Nutrition Society 1984

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