Structural and functional studies on different human FABP types

JH Veerkamp, HTB Van Moerkerk, CFM Prinsen… - Lipid Binding Proteins …, 1999 - Springer
JH Veerkamp, HTB Van Moerkerk, CFM Prinsen, TH Van Kuppevelt
Lipid Binding Proteins within Molecular and Cellular Biochemistry, 1999Springer
Interaction of various ligands with recombinant proteins of 5 human FABP types was studied
by radiochemical and fluorescence procedures. Liver, heart, intestinal and myelin FABP
showed a higher affinity for oleic acid than adipocyte FABP. Intestinal and adipocyte FABP
had a relatively high K d value for arachidonic acid. Liver and intestinal FABP showed high
affinity for DAUDA in contrast to the other FABP types. ANS was only well bound by liver and
adipocyte FABP. Retinol was not bound by any FABP type, retinoic acid only by adipocyte …
Abstract
Interaction of various ligands with recombinant proteins of 5 human FABP types was studied by radiochemical and fluorescence procedures. Liver, heart, intestinal and myelin FABP showed a higher affinity for oleic acid than adipocyte FABP. Intestinal and adipocyte FABP had a relatively high Kd value for arachidonic acid. Liver and intestinal FABP showed high affinity for DAUDA in contrast to the other FABP types. ANS was only well bound by liver and adipocyte FABP. Retinol was not bound by any FABP type, retinoic acid only by adipocyte FABP. Data indicate the importance of both electrostatic and hydrophobic interaction for the ligand-FABP binding. The immunological crossreactivity between six human FABP types including epidermal FABP and their respective antibodies raised in rabbit, chicken and mouse appeared to be low and may suggest heterogeneity of protein surface. (Mol Cell Biochem 192: 137–142, 1999)
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