Modulation of fatty acid-binding capacity of heart fatty acid-binding protein by oxygen — derived free radicals

  • Randall M. Jones
  • M. Renuka Prasad
  • Dipak K. Das
Part of the Developments in Molecular and Cellular Biochemistry book series (DMCB, volume 6)


In this study, we examined the effects of exposure of heart fatty acid-binding protein (h-FABP) to chemically generated O 2 or OH · with respect to its oléate binding and to its electrophoretic properties. Purified rat h-FABP at 40 µlM scavenged as much as 30% O 2 and 85% OH ·. On the other hand, when 2nmol (4µM) FABP were exposed to free radicals, the maximum oleate binding capacity as measured by Scatchard analysis was reduced only by 14% and 27% for O 2 and OH ·, respectively. The electrophoretic pattern of free radical-exposed FABP was not markedly different when examined either by the non-denaturing or by denaturing PAGE, suggesting the absence of any degradation or aggregation of FABP by O 2 or OH ·. It is hypothesized that O 2 or OH · in physiological concentration may not alter the function of FABP markedly in the ischemic-reperfused myocardium.

Key words

heart fatty acid-binding protein free radicals 



Heart Fatty Acid Binding Protein


Non-Esterified Fatty Acids


Superoxide anions

OH ·

hydroxyl radicals


hypohalite radicals


hydrogen peroxide


High Pressure Liquid Chromatography


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Copyright information

© Springer Science+Business Media Dordrecht 1990

Authors and Affiliations

  • Randall M. Jones
    • 1
  • M. Renuka Prasad
    • 1
  • Dipak K. Das
    • 1
  1. 1.Surgical Research Center, Department of Surgery, Cardiovascular DivisionUniversity of Connecticut School of MedicineFarmingtonUSA

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