PURIFICATION AND CHARACTERIZATION OF FATTY-ACID BINDING-PROTEIN FROM AEROBIC MUSCLE OF THE ANTARCTIC ICEFISH CHAENOCEPHALUS-ACERATUS
PURIFICATION AND CHARACTERIZATION OF FATTY-ACID BINDING-PROTEIN FROM AEROBIC MUSCLE OF THE ANTARCTIC ICEFISH CHAENOCEPHALUS-ACERATUS
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DOI：
10.1002/jez.1402730304
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发表时间：
1995-10-15
影响因子：
--
通讯作者：
SIDELL, BD
中科院分区：
文献类型：
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作者：
LONDRAVILLE, RL;SIDELL, BD
胞内脂肪酸结合蛋白是从南极冰鱼Chaenocephalus aceratus有氧骨骼肌中纯化得到的。C.分子量aceratus FABP（CA-FABP）的分子量为14，936 Da，通过电喷雾质谱法估算。CA-FABP以0.984 +/- 0.115 mg CA-FABP g（-1）湿重有氧肌肉的细胞内浓度表达，并在0 ℃的生理温度下结合0.859 +/- 0.013摩尔油酸/摩尔蛋白质。各种脂肪酸配体的解离常数（K（d）s）范围为1.38至2.71 μ M;棕榈酸（16：0）、棕榈油酸（16：1）和油酸（18：1）之间的K（d）s没有显著差异。竞争测定揭示CA-FABP对南极鱼中常见的极长链多不饱和脂肪酸（例如，二十二碳六烯酸; 22：6）。CA-FABP的部分氨基酸序列与哺乳动物心脏型FABP的同源性高达74%。这些数据与哺乳动物的值惊人地相似，但它们来自一种在生殖发育、体温和生理学方面与哺乳动物相距甚远的生物。这表明FABP家族不仅在一级序列上是保守的，而且在其生理特性上也是保守的。(C)1995 Wiley-Liss，Inc.
Intracellular fatty acid-binding protein is purified and characterized from aerobic skeletal muscle of the Antarctic icefish Chaenocephalus aceratus. Molecular mass of C. aceratus FABP (CA-FABP) is 14,936 Da as estimated by electrospray mass spectrometry. CA-FABP is expressed at an intracellular concentration of 0.984 +/- 0.115 mg CA-FABP g(-1) wet weight aerobic muscle and binds 0.859 +/- 0.013 moles oleic acid per mole of protein at a physiological temperature of 0 degrees C. Dissociation constants (K(d)s) for various fatty acid Ligands range from 1.38 to 2.71 mu M; K(d)s are not significantly different among palmitic acid (16:0), palmitoleic acid (16:1), and oleic acid (18:1). Competition assays reveal that CA-FABP does not have preferential affinity for the very-long-chain, polyunsaturated fatty acids that are common in Antarctic fish (e.g., docosahexaenoic acid; 22:6). Partial amino acid sequence from CA-FABP aligns with mammalian heart-type FABPs with as high as 74% identity. These data are strikingly similar to mammalian values, yet they are derived from an organism that is distant from mammals in terms of phylogeny, body temperature, and physiology. This suggests that the FABP family is conserved not only in primary sequence, but also in its physiological properties. (C) 1995 Wiley-Liss, Inc.