Advertisement

Fish Myofibrillar Protein and Lipid Interaction in Aqueous Media as Detected by Isotope Labeling, Sucrose Gradient Centrifugation, Polyacrylamide Electrophoresis and Electron Paramagnetic Resonance

  • Soliman Y. K. Shenouda
  • George M. Pigott
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86A)

Abstract

The integrity and function of various essential natural systems depends on the existence of stable complexes of lipid and protein. Examples of such systems are numerous, such as the fluid mosaic cell membranes, the blood coagulation process, various lipase reactions, actomyosin ATPase activity, blood serum lipoproteins, etc. in food systems, on the other hand, complexes of lipid and protein coexisting naturally, or artificially formed, show an important role in food manufacturing (dough mixing, bread making, dairy products, meat sausage, food emulsions, etc.) and in the instability of processed foods, particularly fishery products.

Keywords

Polar Lipid Neutral Lipid Spin Label Sucrose Gradient Phosphatidyl Choline 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Babbitt, J., Crawford, D.L. and Law, D.K. (1972). Decomposition of TMAO and changes in protein extractability during frozen storage of minced and intact hake muscle. J. Agric. Food Chem., 20:1052.Google Scholar
  2. Berger, K.U., Barratt, M.D. and Kamat, V.B. (1971). Magnetic resonance studies on the components of human erythrocyte membranes. Chem. Phys. Lipids, 6:351.Google Scholar
  3. Borgstrom, G. (1962). Fish as food. Vol. II, Academic Press, N.Y.Google Scholar
  4. Braun, P.E. and Radin, N. (1969). Interaction of lipids with a membrane structural protein. Biochemistry, 8:4310.PubMedCrossRefGoogle Scholar
  5. Bridgen, J. (1972). The reactivity and function of thiol groups in trout actin. Biochem. J., 126:21.Google Scholar
  6. Briskey, E.J. and Fukazawa, T. (1971). Myofibrillar proteins of skeletal muscle. Adv. Food Res., 19:279.PubMedCrossRefGoogle Scholar
  7. Burley, R.W. (1971). Lipoproteins “Biochemistry and methodology of lipids.” Eds. Johnson, A.R. and Davenport, S.P. Wiley. Intersci., N.Y.Google Scholar
  8. Buttkus, H. (1970). Accelerated denaturation of myosin in frozen solution. J. Food Sci., 35:558.CrossRefGoogle Scholar
  9. Camejo, G, Colacicco, G. and Rapport, M.M. (1968). Lipid monolayers: interaction with the apoprotein of high density plasma lipoprotein. J. Lipid Res., 9:562.Google Scholar
  10. Chapman, D., Fluck, D.J., Penkett, S.A. and Shipley, G.G. (1968). Physical studies of phospholipids. 10. The effect of soni-cation on aqueous dispersion of egg yolk lecithin. Biochem. Biophys., Acta, 163:255.Google Scholar
  11. Cherayil, G.D. and Scaria, K.S. (1970). Thin layer chromatography of tissue lipids without extraction. J. Lipid Res., 11:378.Google Scholar
  12. Chrystall, B.B. (1971). Macroscopic, microscopic and physical studies on the influence of heating on muscle tissues and protein. Dissertation Abst., Intl. Sec. B. The Science of Eng., 31:6050. c.f. Fd. Sci. Tech. Abst. (sn2):25189.Google Scholar
  13. Chung Wu, C.S. (1969). Comparative studies on myosin from breast and leg muscles of chicken. Biochemistry, 8:29.Google Scholar
  14. Colacicco, G. and Rapport, M.M. (1966). Lipid monolayers: action of phospholipase-A of Crotalus artox and Naja naja venoms on phosphatidylcholine and phosphatidalcholine. J. Lipid Res., 7:258.Google Scholar
  15. Connell, J.J. (1969). The FPC story VIII on the use of detergents in F.P.C. production. Food Technol., 23:206.Google Scholar
  16. Connell, J.J. (1964). Fish muscle proteins and some effects on them of processing. “Symposium on Foods: Proteins and their reaction.” Eds. Schultz, H.W. and Anglemier, A.F. The AVI Publishing Co., Inc., Conn.Google Scholar
  17. Connell, J.J. (1962). Changes in amount of myosin extractable from cod flesh during storage at-l4°C. J. Sci. Food Agric., 13:607.Google Scholar
  18. Dominova, S.R. (1970). New data on the composition of fish lipids. Food Sci. Technol. Abst., 3(3):3R88.Google Scholar
  19. Drabikowski, W., Kaming, D.R. and Maruyama, K. (1968). Effect of troponin on the reversibility of tropomyosin binding to F-actin. J. Biochem., 63:802.Google Scholar
  20. Dreizen, P. and Gershman, L.C. (1970). Relationship of structure to function in myosin. 2. Salt denaturation and recombination experiments. Biochemistry, 9:1970.Google Scholar
  21. Ebashi, S. and Maruyama, L. ( 1965). Preparation and some properties of α-actinin-free actin. J. Biochem., 58:20.Google Scholar
  22. El-Bastavizi, A.M. and Smirnova, G.A. (1972). Changes of lipid and protein in carp muscle during freezing and frozen storage. c/f Food Sci. Technol. Abst., 5:1R39.Google Scholar
  23. Elzinga, M. (1970). Amino acid sequence studies on rabbit skeletal muscle actin. Cyanogen bromide cleavage of the protein and determination of the sequence of seven of the resulting peptides. Biochemistry, 9:1365.Google Scholar
  24. Folch, J., Lees, M. and Sloanestanley, H.G. (1956). A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem., 2l4:497Google Scholar
  25. Fulk, D.J., Henson, A.F., and Chapman, D. (1969). The structure of dilute lecithin-water system revealed by freeze-etching and electron microscope. J. Ultrastoric. Res., 29:4l6.Google Scholar
  26. Fullington, J.G. (1969). Lipid-protein interaction. Bakers Digest, 43:34Google Scholar
  27. Gillibrand, J.M. (1976). A study of aggregation phenomena occurring in actin solution during polymerization. Biochem. J., 127:737.Google Scholar
  28. Hamm, R. (1966). Heating of muscle systems. “Muscle as a food.” Eds. Briskey, E.J.; Cassens, R.G. and Trautman, J.C. The Univ. of Wisconsin Press, Madison, Wis.Google Scholar
  29. Hao-Chu, G. and Sterling, C. (1970). Parameters of texture changes in processed fish: myosin denaturation. J. Texture Studies, l:2l4.Google Scholar
  30. Helenius, A. and Simon, K. (1972). The binding of detergents to lipophilic and hydrophobic proteins. J. Biol. Chem., 247:3656.Google Scholar
  31. Hendrickson, H.S. and Fullington, J.G. (1965). Stabilities of metal complexes of phospholipids Ca++, Mg++ and Ni++ complex of phosphatidylserine and triphosphoinositide. Biochemistry, 4:1599.Google Scholar
  32. Huszar, G. and Elzinga, M. (1971). Amino acid sequence around the single 3-methylhistidine residue in rabbit skeletal muscle myosin. Biochemistry, 10:229.Google Scholar
  33. Huszar, G. and Elzinga, M. (1969). E-N-Methyl lysine in myosin. Nature, 223:83.CrossRefGoogle Scholar
  34. Johnson, P., Perry, S.V. (1970). Biological activity and 3-methylhistidine content of actin and myosin. Biochem. J., 119:293.Google Scholar
  35. Kimm, S. and Grewther, W.G. (1968). “Symposium on fibrous proteins.” Butterworth, Sydney.Google Scholar
  36. Kuehl, W.M. and Adelstein, R.S. (1970). The absence of 3-methyl-histidine in red cardiac and fetal myosin. Biochim. Biophys. Res. Comm., 39:956.Google Scholar
  37. Lehninger, A.L. (1970). “Biochemistry.” Worth Publishers, Inc., N.Y.Google Scholar
  38. Lovern, J.A. (1956). The lipids of fish. 8. The triglycerides and cholesterol of haddock flesh. Biochem. J., 63:373.PubMedGoogle Scholar
  39. Lowey, S. (1972). Protein assemblies in muscle. “Protein-protein interaction.” Eds. Jaenicke, R. and Helmreich, H., Springer-Verlag, N.Y.Google Scholar
  40. Lowey, S. and Holtzer, A. (1959). The aggregation of myosin. J. Am. Chem. Soc., 81:1378.CrossRefGoogle Scholar
  41. Mao, W.W. and Sterling, C. (1970). Parameters of texture changes in processed fish: cross-linkage of proteins. J. Texture Studies, 1:484.CrossRefGoogle Scholar
  42. Marinette, G.V. and Pettit, D. (1968). The interaction of γ-globu-lin with lipids. Chem. Phys. Lipids, 2:17.CrossRefGoogle Scholar
  43. Olley, J., Farmer, J. and Stephen, E. (1969). The rate of phospholipid hydrolysis in frozen fish. J. Food Technology, 4:27.CrossRefGoogle Scholar
  44. Pitlick, F.A. and Nemerson, Y. (1970). Some technical problems in egg research. Proc. Soc. Anal. Chem., 7:63.Google Scholar
  45. Quinlivan, J., McConnell, H.M., Stowring, L., Cooke, R. and Morales, M.F. (1969). Myosin modification as studied by spin labeling. Biochemistry, 8:3644.PubMedCrossRefGoogle Scholar
  46. Rizzino, A.A., Barouch, W.W., Eisenberg, E., and Moos, C. (1970). Actin-heavy meromyosin binding. Determination of binding stoichiometry from ATP-ase kinetic measurements. Biochemistry, 9:2404.Google Scholar
  47. Robinson, J.D. (1966). Interaction between protein sulphydryl groups and lipid double bonds in biological membranes. Nature, 212:199.Google Scholar
  48. Shenouda, S.Y.K. and Pigott, G.M. (1976). Electron paramagnetic resonance studies of actin-lipid interaction in aqueous media. J. Agric. Food Chem., 24:11.Google Scholar
  49. Shenouda, S.Y.K. and Pigott, G.M. (1975a). Lipid-protein interaction during aqueous extraction of fish-protein: Fish actin preparation and purification. J. Food Sci., 40:520.Google Scholar
  50. Shenouda, S.Y.K. and Pigott, G.M. (1975b). Lipid-protein interaction during aqueous extraction of fish protein: Actin-lipid interaction. J. Food Sci., 40:523.Google Scholar
  51. Shenouda, S.Y.K. and Pigott, G.M. (1974) Lipid protein interaction during aqueous extraction of fish protein. Myosin-lipid interaction. J. Food Sci., 39:726.Google Scholar
  52. Sounders, G. (1968). Molecular aggregation in aqueous dispersion of phosphatidyl and lysophosphatidyl choline. Biochim. Biophys. Acta, 125:70.Google Scholar
  53. Stainier-Lambrecht, A. (1962). Heterogenity of carp L-meromyosin. Arch. Intn. Physid. Biochem., 70:682.Google Scholar
  54. Stansby, M.E. (1967). “Industrial fishery technology.” Reinhol Publishing Corp., Conn.Google Scholar
  55. Suzuki, A. (l9Tl). Denaturation of fish muscle proteins during dehydration. J. Food Sci. Technol. (Japan), 18:l67.Google Scholar
  56. Takama, K., Zama, K. and Igarashi, H. (1972). Changes in the flesh lipids of fish during frozen storage. III. Relation between rancidity in fish flesh and protein extractability. Bull. Jap. Soc. Sci. Fish., 38: 607.CrossRefGoogle Scholar
  57. Trayer, H.R. and Trayer, I.P. (1975). A new and rapid method for the isolation of myosin from small amounts of muscle and non-muscle tissue by affinity chromatography. FEBS Letters, 54:291.Google Scholar
  58. Tsuchiya, T. and Matsumoto, J.J. (1975). Isolation, purification and structure of carp myosin, HMM, and LMM. Bull. Jap. Soc. Sci. Fish., 41:1319.CrossRefGoogle Scholar
  59. Weber, K. and Osborn, M. (1969). The reliability of molecular weight determination by SDS-Polyacrylamide gel electrophoresis. J. Biol. Chem., 244:4406.Google Scholar
  60. Weeds, A.G. (1967). Small sub-units of myosin. Biochem. J., 105:25C.Google Scholar
  61. Wessels, J.P.H. and Spark, A.A. (1973). The fatty acid composition of the lipids from two species of hake. J. Sci. Food Agric., 24:1939.Google Scholar
  62. Wood, G. and Hintz, L. (1971). Lipid changes associated with the degradation of fish tissue. J. Assoc. Off. Anal. Chem., 54:1019.Google Scholar
  63. Wu, C.S. and Sayre, R.N. (1971). Myosin stability in intact chicken muscle and a protein component released after aging. J. Food Sci., 36:133.Google Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Soliman Y. K. Shenouda
    • 1
  • George M. Pigott
    • 2
  1. 1.National Marine Fisheries ServiceGloucesterUSA
  2. 2.Institute for Food Science and TechnologyCollege of Fisheries, University of WashingtonSeattleUSA

Personalised recommendations