Interaction of rat alpha-fetoprotein and albumin with polyunsaturated and other fatty acids: determination of apparent association constants

FEBS Lett. 1989 Jun 19;250(1):22-4. doi: 10.1016/0014-5793(89)80676-3.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Fatty Acids, Nonesterified / metabolism*
  • Fatty Acids, Unsaturated / metabolism*
  • Kinetics
  • Protein Binding
  • Rats
  • Serum Albumin / metabolism*
  • alpha-Fetoproteins / metabolism*

Substances

  • Fatty Acids, Nonesterified
  • Fatty Acids, Unsaturated
  • Serum Albumin
  • alpha-Fetoproteins