ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    The dual location of β-oxidation enzymes in germinating pea cotyledons (1986)
    Springer
    Planta 167 (1986), S. 54-57 
    Details
    ISSN: 1432-2048
    Keywords: β-Oxidation (enzyme location) ; Mitochondrion ; Microbody ; Pisum (β-oxidation)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract β-Oxidation enzymes were detected both in the mitochondria and microbodies of pea cotyledons. Intact mitochondria did not show β-oxidation enzyme activity but in ruptured mitochondria this activity was high. It is apparent that the mitochondrial membrane barrier prevents rapid access of acyl-CoA substrates to matrix β-oxidation sites. Removal of the membrane barrier permits rapid access of acyl-CoAs and these enzyme activities may then be measured.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446368
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...