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

Abstract:

:In this study, we examined the effects of exposure of heart fatty acid-binding protein (h-FABP) to chemically generated O2- or OH. with respect to its oleate binding and to its electrophoretic properties. Purified rat h-FABP at 40 microM scavenged as much as 30% O2- and 85% OH.. On the other hand, when 2 nmol (4 microM) FABP were exposed to free radicals, the maximum oleate binding capacity as measured by Scatchard analysis was reduced only by 14% and 27% for O2- 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 O2- or OH.. It is hypothesized that O2- or OH. in physiological concentration may not alter the function of FABP markedly in the ischemic-reperfused myocardium.

journal_name

Mol Cell Biochem

authors

Jones RM,Prasad MR,Das DK

doi

10.1007/BF00231380

subject

Has Abstract

pub_date

1990-10-15 00:00:00

pages

161-6

issue

1-2

eissn

0300-8177

issn

1573-4919

journal_volume

98

pub_type

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