Search
Filter Results
- Resource Type
- Article1
- Journal1
- Journal Digital1
- Article Type
- Comparative Study1
- Result From
- Lane Catalog1
- PubMed1
-
Year
- Journal Title
- J Biochem1
Search Results
Sort by
- JournalDigital AccessProviderVersionSpringerCINAHLv. 1-, 1994- Full text delayed 12 monthsAcad Search Premv. 1-, 1994- Full text delayed 12 months
- ArticleShindo Y, Hashimoto T.J Biochem. 1978 Nov;84(5):1177-81.Rat liver peroxisomes oxidized palmitate in the presence of ATP, CoA and NAD+, and the rate of palmitate oxidation exceeded that of palmitoyl-CoA oxidation. Acyl-CoA synthetase [acid: CoA ligase (AMP-forming); EC 6.2.1.3] was found in peroxisomes. The substrate specificity of the peroxisomal synthetase towards fatty acids with various carbon chain lengths was similar to that of the microsomal enzyme. The peroxisomal synthetase activity toward palmitate (40--100 nmol/min per mg protein) was higher than the rate of palmitate oxidation by the peroxisomal system (0.7--1.7 nmol/min per mg protein). The data show that peroxisomes activate long chain fatty acids and oxidize their acyl-CoA derivatives.