Chemical Structure and Physiological Function of Hydrophobic Molecule-binding Protein in Cytosols

研究了细胞质中疏水分子结合蛋白的结构、功能关系和细胞分布.鉴定了一种新的大鼠肝脏脂肪酸结合蛋白，其105位为异戊酰残基，并探讨了其生理意义.合成了光敏亲和标记物，并用于鉴定脂肪酸结合蛋白中的疏水配体结合位点。油酰咪唑也被合成，并被证明是一个有效的亲和标记的脂肪酸结合区.一种疏水性致癌染料，氨基偶氮苯，给予大鼠和结合位点，其代谢活化的产品进行了鉴定。另外还鉴定了两个结合蛋白.从肠上皮细胞中分离到一个新的疏水分子结合蛋白，并进行了全序列测定.从大鼠肾脏中分离到两种脂肪酸结合蛋白。结果表明，其中一个是脂质运载蛋白超家族成员，另一个是心脏型脂肪酸结合蛋白。

Hydrophobic molecule-binding proteins in cytosols were investigated for their structure and function relationship and for cellular distribution.1. A novel molecular species of rat liver fatty acid binding protein having isoaspartyl residue at position 105 was identified and its physiological significance was investigated.2. Photo-sensitive affinity labels were synthesized and used for identification of hydrophobic ligand-binding site(s) in fatty acid binding protein. Oleoylimidazolide was also synthesized and shown to be an effective affinity-label for fatty acid binding region.3. A hydrophobic carcinogenic dye, amino-azobenzene, was administered to rats and binding site for its metabolically activated product was identified. Two other binding proteins were also identified.4. A new hydrophobic molecule-binding protein was isolated from intestinal epithelium and fully sequenced.5. Two fatty acid binding proteins were isolated from rat kidneys. It was shown that one of them is a member of lipocalin superfamily and the other heart type fatty acid binding protein.