2-Methylbutyryl-CoA: succinate acyl-CoA transferase activity and function in Ascaris suum muscle

A branched-chain acyl-CoA transferase activity which transfers coenzyme A from either 2-methylbutyryl or 2-methylvaleryl-CoA to succinate is present in the muscle mitochondria from the intestinal nematode, Ascaris suum. Its physiological function is discussed. This activity appears to differ from th... Ausführliche Beschreibung

1. Person: Saz, H.J.
Weitere Personen: deBruyn, B.S.
Quelle: in Comparative Biochemistry and Physiology -- Part B: Biochemistry and Vol. 108, No. 4 (1994), p. 513-519
Weitere Artikel
Format: Online-Artikel
Sprache: English
Veröffentlicht: 1994
Beschreibung: Online-Ressource
Schlagworte: Coenzyme A
Transacylase
Succinate
Propionate
2-Methylbutyrate
2-Methylvalerate
Ascaris
Nematode
Mitochondria
Online Zugang: Online
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Anmerkung: Copyright: Copyright (c) 2002 Elsevier Science Inc.
Zusammenfassung: A branched-chain acyl-CoA transferase activity which transfers coenzyme A from either 2-methylbutyryl or 2-methylvaleryl-CoA to succinate is present in the muscle mitochondria from the intestinal nematode, Ascaris suum. Its physiological function is discussed. This activity appears to differ from the previously described acetyl-CoA:propionate and propionyl-CoA:succinate acyl-CoA transferases on the basis of heat stability, substrate specificity and the requirement of a ''factor'' from boiled Ascaris mitochondria for optimal activity of only the branched-chain acyl-CoA transferase. The ''factor'' has been recovered from HPLC and some of its properties examined. It could not be replaced by a crude soluble fraction from rat liver mitochondria, or by adenine, guanine or inosine di- or triphosphates. Activity was lost upon ashing, but was not affected by treatment with either pepsin or chymotrypsin.
ISSN: 0305-0491

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