Human liver fatty acid binding protein cDNA and amino acid sequence. Functional and evolutionary implications.
Human liver fatty acid binding protein cDNA and amino acid sequence. Functional and evolutionary implications.
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DOI：
10.1016/s0021-9258(18)89406-6
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发表时间：
1985-03
期刊：
影响因子：
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通讯作者：
Lgwrence ChanSQ;Chik-Fong WeiSQ;Wen-Hsiung Lin;Chao-Yuh YangQ;Paul RatnerSQ;Henry PownallQ;Antonio M. Gotto;Louis C. SmithSQII
中科院分区：
文献类型：
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作者：
Lgwrence ChanSQ;Chik-Fong WeiSQ;Wen-Hsiung Lin;Chao-Yuh YangQ;Paul RatnerSQ;Henry PownallQ;Antonio M. Gotto;Louis C. SmithSQII
在肝脏 cDNA 文库中鉴定了人肝脏脂肪酸结合蛋白 (L-FABP) cDNA 克隆。两个最长的克隆已完全测序。核苷酸序列预测蛋白质有 127 个氨基酸残基。通过纯化的人 L-FABP 肽的有限氨基酸序列分析和放射性标记的体外翻译的 FABP 的 Edman 降解来证实克隆的身份。对人L-FABP、大鼠L-FABP、大鼠肠(I-) FABP和小鼠422蛋白的氨基酸和mRNA序列的统计分析表明，人和大鼠L-FABP高度同源，并且L-FABP和I-FABP在很久以前(大约650-6.9亿年前)就出现了分歧，尽管它们彼此之间的关系比它们与422蛋白中的任何一个都更密切。对人和大鼠 L-FABP 一级序列的二级结构预测揭示了一个区域（残基 12-30），该区域可能是两个 L-FABP 的假定脂肪酸结合域。了解 L-FABP 的一级氨基酸序列和可能的功能域对于进一步定义和理解该蛋白质的配体结合和转移机制至关重要。
Human liver fatty acid binding protein (L-FABP) cDNA clones were identified in a liver cDNA library. The two longest clones were completely sequenced. The nucleotide sequence predicts a protein of 127 amino acid residues. Identity of the clones was confirmed by limited amino acid sequence analysis of purified human L-FABP peptides and Edman degradation of radiolabeled in vitro translated FABP. Statistical analysis of the amino acid and mRNA sequences of human L-FABP, rat L-FABP, rat intestinal (I-) FABP, and mouse 422 protein indicates that the human and rat L-FABPs are highly homologous and that L-FABP and I-FABP diverged a long time ago (approximately 650-690 million years ago), although they are more closely related to each other than either of them is to 422 protein. Secondary structure predictions from the primary sequence of human and rat L-FABP reveal a region (residues 12-30) that might be the putative fatty acid binding domain of the two L-FABPs. Knowledge of the primary amino acid sequence of L-FABP and possible functional domains will be pivotal in further defining and understanding the mechanism of ligand binding and transfer by this protein.