Structural and functional studies on different human FABP types

被引:85
作者
Veerkamp, JH [1 ]
van Moerkerk, HTB [1 ]
Prinsen, CFM [1 ]
van Kuppevelt, TH [1 ]
机构
[1] Univ Nijmegen, Dept Biochem, NL-6500 HB Nijmegen, Netherlands
关键词
fatty acid-binding protein; myelin FABP; 11-dansylamino-undecanoic acid; 1-anilinonaphtalene-8-sulfonic acid; retinoic acid; immunological crossreactivity;
D O I
10.1023/A:1006866119264
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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 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.
引用
收藏
页码:137 / 142
页数:6
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