Modulation of fatty acid-binding capacity of heart fatty acid-binding protein by oxygen — derived free radicals
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 wordsheart fatty acid-binding protein free radicals
Heart Fatty Acid Binding Protein
Non-Esterified Fatty Acids
- OH ·
- OCI ·
High Pressure Liquid Chromatography
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