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  • metabolic channelling  (1)
  • phospholipids  (1)
  • Springer  (2)
  • 1
    ISSN: 1573-4919
    Keywords: mitochondria ; creatine kinase ; adenylate kinase ; compartmentation ; oncotic pressure ; metabolic channelling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Cytosolic proteins as components of the physiological mitochondrial environment were substituted by dextrans added to media normally used for incubation of isolated mitochondria. Under these conditions the volume of the intermembrane space decreases and the contact sites between the both mitochondrial membranes increase drastically. These morphological changes are accompanied by a reduced permeability of the mitochondrial outer compartment for adenine nucleotides as it was shown by extensive kinetic studies of mitochondrial enzymes (oxidative phosphorylation, mi-creatine kinase, mi-adenylate kinase). The decreased permeability of the mitochondrial outer membrane causes increased rate dependent concentration gradients in the micromolar range for adenine nucleotides between the intermembrane space and the extramitochondrial space. Although all metabolites crossing the outer membrane exhibit the same concentration gradients, considerable compartmentations are detectable for ADP only due to its low extramitochondrial concentration. The consequences of ADP-compartmentation in the mitochondrial intermembrane space for ADP-channelling into the mitochondria are discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 183 (1998), S. 169-173 
    ISSN: 1573-4919
    Keywords: hexadecylphosphocholine ; phospholipases ; inhibition ; rat liver mitochondria ; phospholipids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Hexadecylphosphocholine (HePC) is known as antitumor agent but the mechanism has not yet been understood. In rat liver mitochondria its effect on phospholipid transformation has been studied by quantitative HPTLC and phosphorus determination. From the results it can be concluded that HePC influences the activities of phospholipase A2, phospholipase C, phospholipase D, and lysophospholipase A. The phospholipid transformation as well as the influence of HePC are affected by exogenous calcium ions. In the presence of calcium HePC has been found to inhibit enzyme activities, whereas in the absence of exogenous calcium ions enzymatic phospholipid transformations are activated or inhibited depending on HePC concentrations.
    Type of Medium: Electronic Resource
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