Key result
Rat alpha-fetoprotein binds docosahexaenoic acid with ~50-fold higher affinity than albumin.
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The interaction of fatty acids with rat alpha-fetoprotein and albumin was measured using a partition equilibrium method. alpha-Fetoprotein (AFP) displays one high-affinity binding site for fatty acids and albumin near two binding sites. The AFP association constants for most fatty acids were similar to those of albumin (in the 10(7) M-1 range) whereas for docosahexaenoic acid it was 9.7 x 10(8) M-1, about 50-fold higher than that corresponding to albumin. This difference justifies docosahexaenoic acid in fetal or neonatal serum being mainly bound to AFP and can indicate a highly specific role of AFP in the transport of this fatty acid.
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Anel et al. (1989) studied this question. Rat alpha-fetoprotein vs. Rat albumin was evaluated on Apparent association constants for fatty acids. Rat alpha-fetoprotein bound docosahexaenoic acid with an association constant of 9.7 x 10^8 M^-1, about 50-fold higher than that of albumin.
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