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

研究了细胞溶胶中疏水分子结合蛋白的结构、功能关系和细胞分布。鉴定了一个105位有异天冬氨酸残基的大鼠肝脏脂肪酸结合蛋白的新分子种，并对其生理意义进行了研究。合成了光敏亲和标签，用于脂肪酸结合蛋白疏水配体结合位点的鉴定。合成了油酰咪唑烷，并证明它是一种有效的脂肪酸结合区亲和标记。一种疏水致癌染料氨基偶氮苯给药于大鼠，并确定了其代谢激活产物的结合位点。另外两种结合蛋白也被鉴定出来。从肠上皮中分离到一种新的疏水分子结合蛋白，并对其进行了完整的测序。从大鼠肾脏中分离出两种脂肪酸结合蛋白。结果表明，其中一个是脂钙蛋白超家族成员，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.