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Influence of dietary leucine content on the activities of branched-chain amino acid aminotransferase (EC 2.6.1.42) and branched-chain α-keto acid dehydrogenase (EC 1.2.4.4) complex in tissues of preruminant lambs

Published online by Cambridge University Press:  09 March 2007

Isabelle Papet ,
Nadia Lezebot ,
Francoise Barre ,
Maurice Arnal  and
Alfred E. Harper
Isabelle Papet
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté-INRA Theix, 63122 Ceyrat, France
Nadia Lezebot
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté-INRA Theix, 63122 Ceyrat, France
Francoise Barre
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté-INRA Theix, 63122 Ceyrat, France
Maurice Arnal
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté-INRA Theix, 63122 Ceyrat, France
Alfred E. Harper
Affiliation:
Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA
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Abstract

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1. Branched-chain amino acid aminotransferase (EC 2.6.1.42; BCAAT) and branched-chain α-keto acid dehydrogenase (EC 1.2.4.4; BCKDH) activities were measured in preruminant lamb liver, longissimus dorsi muscle, kidney, jejunum and adipose tissue, 2 h after a meal with or without an excess of leucine.

2. Skeletal muscle contained about 70% of the total basal BCAAT activities of the tissues studied whereas liver contained about 60% of the total BCKDH activities of these tissues.

3. BCAAT activities were very low in preruminant lamb tissues. BCKDH was more phosphorylated in tissues of preruminant lambs than in rats, especially in liver. These low catalytic potentialities might contribute to a low rate of branched-chain amino acid catabolism in sheep.

4. Ingestion of an excess of leucine led to an increase in liver and jejunum BCAAT activities and activation of BCKDH in jejunum.

Type
Research Article
Information
British Journal of Nutrition , Volume 59 , Issue 3 , May 1988 , pp. 475 - 483
Copyright
Copyright © The Nutrition Society 1988

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