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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)

Summary

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 

Abbreviations

h-FABP

Heart Fatty Acid Binding Protein

NEFA

Non-Esterified Fatty Acids

O2

Superoxide anions

OH ·

hydroxyl radicals

OCI ·

hypohalite radicals

H2O2

hydrogen peroxide

HPLC

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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