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Association of Malonaldehyde with Rabbit Myosin Subfragment 1

  • A. J. King
  • S. J. Li

Abstract

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

Keywords

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.

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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

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