Association of Malonaldehyde with Rabbit Myosin Subfragment 1

  • A. J. King
  • S. J. Li


Scientists have noted that after storage, previously ground poultry meat looses some functional properties. Part of the change in functionality of protein of previously ground and frozen meat may be due to accelerated lipid deterioration. Malonaldehyde, a by-product of lipid oxidation, could react with specific amino acids in protein to produce a Schiff’s base, thereby altering the structure and ultimately the functionality of protein. Investigations on rabbit myosin subfragment 1 and malonaldehyde were conducted to establish a link between lipid deterioration and deceased functionality of myosin. Accelerated lipid oxidation decreased myosin ATPase activity and caused conformational changes as measured by sulfhydryl content, protein bound malonaldehyde, tryptophan fluorescence, and 1-anilino-8-napthalenesulfonate fluorescence. There was a positive correlation between decreases in ATPase activity and increases in incubation time


ATPase Activity Lipid Oxidation Freeze Storage Myofibrillar Protein Tryptophan Fluorescence 
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. Acton, J.C. Restructuring in further processed turkey products. Turkey World 1983 58, 13–16Google Scholar
  2. Andou, S.; Takama, K.; Zama, K. Interaction between lipid and protein during frozen storage. II. Effect of non-polar and polar lipid on rainbow trout myofibrils during frozen storage. Bull. Fac. Fish. Hokkaido Univ 1980 31, 201–209Google Scholar
  3. Andrews, F.; Bjorksten, J.; Trenk, F.B. The reaction of an autoxidized lipid with proteins. J. Ame. Oil Chem. Soc 1965 42, 779–781CrossRefGoogle Scholar
  4. Aruoma, O.I.. Free radicals, oxidative stress, and antioxidants in human health and disease. J. Ame Oil Chem Soc 1998, 75,199–212CrossRefGoogle Scholar
  5. Benedetti, A.; Casini, A.F.; Ferrali, M.; Comportin, M. Extraction and partial characterization of dialyzable products originating from the peroxidation of liver microsomal lipids and inhibiting microsomal glucose-6phosphatase activity. Biochem. Pharmacol 1979 28, 2909–2918CrossRefGoogle Scholar
  6. Bertazzon, A.; Tian, G.H.; Lamblin, A.; Tsong, T.Y. Enthalpic and entropie contributions to actin stability: Calorimetry, circular dichroism, and fluorescence study and effect of calcium. Biochemistry 1990 29, 291–298CrossRefGoogle Scholar
  7. Braddock, R.J.; Dugan, L.R. Jr. Reaction of autoxidizing linoleate with coho salmon myosin. J. Am. Oil Chem. Soc 1973 50, 343–347CrossRefGoogle Scholar
  8. Buttkus, H. The reaction of myosin with malonaldehyde. J. Food Sci 1967 32, 432–434CrossRefGoogle Scholar
  9. Decker, E.A.; Xiong, Y.L.; Calvert, J.T.; Crum, A.D.; Blanchard, S.P. Chemical, physical, and functional properties of oxidized turkey white muscle myofibrillar proteins. J. Agric Food Chem 1993 1, 186–189CrossRefGoogle Scholar
  10. Di Mont, D.; Ross, D.; Bellomo, G.; Eklow, L.; Orrenius, S. Alteration in intracellular thiol homeostasis during the metabolism of menadione by isolated rat hepatocytes. Arch Biochem. Biophy 1984 235, 334–342CrossRefGoogle Scholar
  11. Esterbauer, H.; Cheeseman, K.H., Eds. “Lipid Peroxidation, Chemistry and Physical Properties of Lipids”. Vol. 44; 45. Special issue. Elsevier, Amesterdam, 1987Google Scholar
  12. Esterbauer, H.; Schaur, R.J.; Zollner, H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radical Biol & Med 1991 I1, 81–128CrossRefGoogle Scholar
  13. Funes, J.A.; Weiss, U.; Karel, M. Effect of reaction conditions and reactant concentrations on polymerization of lysozyme reacted with peroxidizing lipids. J Agric Food Chem 1982 30, 1204–1208CrossRefGoogle Scholar
  14. Hultin, H.O. Characteristics of muscle tissue. In Food Chemistry; Fenema, O.R., Ed.; Dekker: New York, 1985; Chapter 12, pp 725–789Google Scholar
  15. Kanner, J.; Karel, M. Change of lysozyme due to reaction with peroxidizing methyl linoleate in dehydrated model system. J. Agric. Food Chem 1976 24, 468–472CrossRefGoogle Scholar
  16. Li, S.J.; King, A.J. Lipid oxidation and myosin denaturation in dark chicken meat. J. Agric. Food Chem 1996 44, 3080–3084CrossRefGoogle Scholar
  17. Lin, W.S.; Armstrong, D.A.; Gaucher, G.M. Formation and repair of papain sulfenic acid. Can J. Biochem 1975 53, 298–307CrossRefGoogle Scholar
  18. Liu, G.; Xiong, Y.L. Storage stability of antioxidant-washed myofibrils from chicken white and red muscle. J. Food Sci 1996 61, 890–894CrossRefGoogle Scholar
  19. Logani, M.K.; Davies, R.E. Lipid oxidation: Biological effects and antioxidants-A review. Lipids 1980 15, 485–495CrossRefGoogle Scholar
  20. Lowry, O.H.; Rosebrough, N.J.; Farr, A.L.; Randall, R.J. Protein measurement with the Folin phenol reagent J. Biol. Chem 1951 193, 265–275Google Scholar
  21. McKeith, F.K.; Bechtel, P.J.; Novakofsi, J.; Park, S.; Arnold, J.S. Characteristics of surimi-like material from beef, pork, and beef by-products. Proc. Int. Congress Meat Sci. Technol 1988 34(B), 325–326Google Scholar
  22. Nakhost, Z.; Karel, M. Change of bovine myoglobin due to interaction with methyl linoleate in a model system. J. Food Sci 1983 48, 1335–1339CrossRefGoogle Scholar
  23. Raharjo, S.; Sofos, J.N.; Schmidt, G.R. Solid-phase acid extraction improves thiobarbituric acid method to determine lipid oxidation. J. Food Sci 1993 58, 921–924CrossRefGoogle Scholar
  24. Riley, M.; Harding, J.J. The reaction of malonaldehyde with lens proteins and the protective effect of aspirin. Biochim et Biophys Acta 1993 1158, 107–112CrossRefGoogle Scholar
  25. Shenouda, S.Y.K. Theories of protein denaturation during frozen storage of fish flesh. Vol. 26. In Advances in Food Research; Chichester, C.O., Ed.; Academic press: New York, N.Y. 1980; pp 275–311Google Scholar
  26. Shimasaki, H.; Ueta, N.; Privett, O.S. Covalent binding of peroxidized linoleic acid to protein and amino acids as models for lipofuscin formation. Lipids 1982 17, 878–883CrossRefGoogle Scholar
  27. Sikorski, Z.E. Protein changes in muscle foods due to freezing and protein storage. Int J. Refrigeration 1978 1, 174–180CrossRefGoogle Scholar
  28. Smith, D.M. Functional and biochemical changes in debonded turkey due to frozen storage and lipid oxidation. J. Food Sci 1987 52,22–27CrossRefGoogle Scholar
  29. Smyth, A.B.; Smith, D.M.; Vega-Warner, V.; O’Neill, E. Thermal denaturation and aggregation of chicken breast muscle myosin and subfragments. J. Agric Food Chem 1996 44, 1005--1010CrossRefGoogle Scholar
  30. Srinivasan, S.; Xiong, Y.; Decker, E.A. Inhibition of protein and lipid oxidation in beef heart surimi-like material by antioxidants and combinations of pH, NaCI, and buffer type in the washing media. J. Agric. Food Chem 1996 44, 119–125CrossRefGoogle Scholar
  31. Tappel, A.L.; Roubel, W.T. Damage of protein enzymes and amino acids by peroxidizing lipids. Arch. Biochem. Biophys 1966 113, 5–8CrossRefGoogle Scholar
  32. Tong, S.W.; Elzinga, M. Amino acids sequence of rabbit skeletal muscle myosin. J. Bin Chem 1990 265, 4893–4901Google Scholar
  33. Wan, L.; Xiong, Y.L.; Decker, E.A. Inhibition of oxidation during washing improves the functionality of bovine cardiac myofibrillar protein. J. Agric Food Chem 1993 41, 2267–2271CrossRefGoogle Scholar
  34. Wang, B.; Xiong, Y.L.; and Srinivasan, S. Chemical stability of antioxidant-washed beef heart surimi during frozen storage. J. Food Sci 1997 62, 939–945, 991CrossRefGoogle Scholar
  35. Wells, J.A.; Moshe, M.; Yount, R.G. Inactivation of myosin subfragment one by cobalt (II)/cobalt (IlI) phenanthroline complexes. 2. Cobalt chelation of two critical SH groups. Biochemistry 1979 18, 4800–4805CrossRefGoogle Scholar
  36. Xiong, Y.L.; Decker, E.A.; Robe, G.H.; Moody, W.G. Gelation of crude myofibrillar protein isolated from beef heart under antioxidative conditions. J. Food Sci 1993 58, 1241–1244CrossRefGoogle Scholar
  37. Xiong, Y.L and Blanchard, S.P. Rheological properities of salt-soluble protein from white and red skeletal muscles. J. Agric Food Chem 1994 42, 1624–1628CrossRefGoogle Scholar
  38. Yeo, H.C.; Helbock, H.J.; Chyu, D.W.; Ames, B.N. Assay of malonaldehyde in biological fluids by gas chromatography-mass spectrometry. Anal Biochem 1994 220, 391–396CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • A. J. King
    • 1
  • S. J. Li
    • 1
  1. 1.Department of Avian SciencesUniversity of CaliforniaDavisUSA

Personalised recommendations