A Unique Role of Histidine in Fe-Catalyzed Lipid Oxidation by Fish Sarcoplasmic Reticulum

  • Marilyn C. Erickson
  • Herbert O. Hultin
Part of the Basic Life Sciences book series (BLSC, volume 49)


The sarcoplasmic reticulum (SR) fraction of fish muscle contains an enzymic lipid peroxidation system requiring NADH and Fe that is stimulated by ADP.1,2 Although in these and other studies, concentrations of metabolites used are representative of the conditions in situ, the amount of Fe is present at a much higher concentration than would normally occur in tissues, e.g., Fe in the low molecular weight fraction of flounder muscle is <3% of total iron.3 Thus, the amount and state of the Fe is most probably a rate limiting factor in lipid oxidation in situ. A large number of 0- N-, and S-containing compounds are capable of binding Fe in either the Fe+2 or Fe+3 states, and it is likely, therefore, that Fe is not found free in vivo but is bound to these cellular metabolites. Chelation of Fe is important in lipid oxidation in vitro since it may keep the Fe soluble or change its oxidation-reduction potential. In this study, we demonstrate that the free amino acid histidine can either enhance or inhibit Fe-catalyzed lipid oxidation to a significant degree. The effect of histidine is determined in part by the presence of a nucleotide.


Sarcoplasmic Reticulum Lipid Oxidation Lipid Peroxidative Activity Sarcoplasmic Reticulum Protein Ascorbate Ferrous 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    M. Borhan, R.L. Shewfelt, and H.O. Hultin, Sarcoplasmic reticulum from flounder muscle having improved lipid peroxidative activity, Anal. Biochem. 137:58 (1984).PubMedCrossRefGoogle Scholar
  2. 2.
    R.E. McDonald and H.O. Hultin, Some characteristics of the enzymic lipid peroxidation system in the microsomal fraction of flounder skeletal muscle, J. Food Sci. 52:15 (1987).CrossRefGoogle Scholar
  3. 3.
    K.M. Kramer, Form of iron in flounder muscle and its relation to sarcoplasmic reticular lipid oxidation, M.S. Thesis, University of Massachusetts, Amherst (1987).Google Scholar
  4. 4.
    J.A. Buege and S.D. Aust, Microsomal lipid peroxidation, in: “Methods in Enzymology,” Vol. 52, S. Fleischer and L. Packer, eds., Academic Press, NewYork, p. 302 (1978).Google Scholar
  5. 5.
    M.A.K. Markwell, S.M. Hass, L.L. Bieber, and N.E. Tolbert, Modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87:206 (1978).PubMedCrossRefGoogle Scholar
  6. 6.
    E. Graf, J.R. Mahoney, R.G. Bryant, and J.W. Eaton, Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site, J. Biol. Chem. 259:3620 (1984).PubMedGoogle Scholar
  7. 7.
    N.H. Kolodny and L.J. Collins, Proton and phosphorus-31 NMR study of the dependence of diadenosine tetraphosphate conformation on metal ions. J. Biol. Chem. 261:14571 (1986).PubMedGoogle Scholar
  8. 8.
    S. Ikeda, Other organic components and inorganic components, in: “Advances in Fish Science and Technology,” J.J. Connell, ed., Fishing News Books Ltd., Surrey, England, p. 111 (1980).Google Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Marilyn C. Erickson
    • 1
  • Herbert O. Hultin
    • 1
  1. 1.Massachusetts Agricultural Experiment Station Department of Food Science and Nutrition Marine Foods LaboratoryUniversity of MassachusettsGloucesterUSA

Personalised recommendations