Kuo T M, Ohlrogge J B
Arch Biochem Biophys. 1984 Oct;234(1):290-6. doi: 10.1016/0003-9861(84)90351-5.
Acyl carrier protein (ACP) from spinach leaves has been purified to homogeneity by high-performance liquid chromatography with an anion-exchange column. The amino acid sequence of one major ACP in spinach leaves, ACP-I, has been determined by automated Edman degradation. It consists of the following 82 amino acids: (sequence in text). Sequencing of the intact polypeptide provided data for the first 57 residues. Cleavage of the succinylated ACP with CNBr at Met-46, followed by sequencing of the fragment mixture, provided data for the final 36 residues. The C-terminal alanine was confirmed by carboxypeptidase Y digestion. The spinach ACP has 40, 70, and 25% homology with Escherichia coli, barley, and rabbit ACPs, respectively. The results not only provide the first complete sequence of a plant ACP, but also provide insight into the structural and evolutionary relationships among plant, animal, and bacterial ACPs.
菠菜叶中的酰基载体蛋白（ACP）已通过阴离子交换柱的高效液相色谱法纯化至同质。菠菜叶中一种主要的ACP（ACP-I）的氨基酸序列已通过自动Edman降解法确定。它由以下82个氨基酸组成：（文中序列）。完整多肽的测序提供了前57个残基的数据。用溴化氰在Met-46处切割琥珀酰化的ACP，然后对片段混合物进行测序，提供了最后36个残基的数据。通过羧肽酶Y消化确认了C末端的丙氨酸。菠菜ACP与大肠杆菌、大麦和兔ACP的同源性分别为40%、70%和25%。这些结果不仅提供了植物ACP的首个完整序列，还深入了解了植物、动物和细菌ACP之间的结构和进化关系。
