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  • 1
    Electronic Resource
    Electronic Resource
    β-Oxidation enzymes in the mitochondria of Arum and oilseed rape (1990)
    Springer
    Planta 182 (1990), S. 129-135 
    Details
    ISSN: 1432-2048
    Keywords: Arum ; Brassica (β-oxidation) ; β-Oxidation ; (enzyme location) ; Microbody ; Mitochondrion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract β-Oxidation enzymes were detected both in the mitochondria and microbodies of Arum maculatum L. spadices and Brassica napus L. seeds. It is apparent that the mitochondrial membrane barrier, which remains intact after sucrose-density-gradient centrifugation, prevents rapid access of acyl-GoA substrates to matrix βoxidation tes. Thus intact mitochondria showed little β-oxidation enzyme activity. Rupturing of the mitochondrial membrane allowed rapid access of acyl CoAs to matrix sites. Consequently, in ruptured mitochondria, high β-oxidation enzyme activities were measured.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00239994
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  • 2
    Electronic Resource
    Electronic Resource
    The two β-oxidation sites in pea cotyledons (1986)
    Springer
    Planta 168 (1986), S. 261-266 
    Details
    ISSN: 1432-2048
    Keywords: Carnitine palmitoyltransferase (location, function) ; Cotyledon (β-oxidation) ; Microbody ; Mitochondrion ; β-Oxidation ; Pisum (β-oxidation)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two sites for β-oxidation of fatty acids in pea (Pisum sativum L.) cotyledons exist. One site is the microbody, the other the mitochondrion. Mitochondrial β-oxidation of fatty acids is carnitine-dependent. The fatty acid permeates the membrane as palmitoylcarnitine which is formed from cytosolic-side palmitoyl-CoA by a carnitine palmitoyltransferase located on the exterior face of the inner mitochondrial membrane as a peripheral protein. A single-gated pore integral membrane translocator is proposed to exchange the palmitoylcarnitine for carnitine or acetylcarnitine across the membrane. An internal (matrix side) carnitine palmitoyltransferase then reforms palmitoyl-CoA which enters β-oxidation and subsequently the tricarboxylic-acid cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402972
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  • 3
    Electronic Resource
    Electronic Resource
    Long-chain acyl CoA synthetase, carnitine and β-oxidation in the pea-seed mitochondrion (1988)
    Springer
    Planta 173 (1988), S. 263-266 
    Details
    ISSN: 1432-2048
    Keywords: Carnitine ; Carnitine palmitoyltrans-ferase ; Long-chain acylCoA synthetase ; Mitochondrion (outer membrane) ; Mitoplast ; β-Oxidation ; Palmitate ; PalmitoylCoA ; Pisum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mitochondria from pea (Pisum sativum L.) seeds were separated into two fractions, mitoplasts (intact inner membrane) and the outer-membrane fraction. The mitoplasts only oxidised palmitate in the presence of carnitine and added outermembrane fraction. Mitoplasts were able to oxidise palmitoylCoA in the presence of carnitine and added outer-membrane fraction had no effect on this oxidation. It was concluded that a long-chain acylCoA synthetase (EC 6.2.1.3) was located on the outer membrane and that the activity of this enzyme in assays was more than sufficient to account for any observed rate of O2 uptake during palmitate oxidation by pea mitochondria. The location of carnitine long-chain acyltransferase (carnitine palmitoyl transferase EC 2.3.1.21) would appear to be the mitoplast i.e. the inner mitochondrial membrane, and confirms the previous work at Newcastle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403019
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