Bouillon P, Drischel C, Vergnolle C, Duranton H, Kader J C
Eur J Biochem. 1987 Jul 15;166(2):387-91. doi: 10.1111/j.1432-1033.1987.tb13527.x.
The complete amino acid sequence phospholipid-transfer protein isolated from spinach leaves has been determined. The primary structure of the spinach protein was elucidated by analyses by HPLC of cyanogen bromide fragments and peptides obtained by tryptic digestions. The single polypeptide chain of the spinach protein consists of 91 amino acid residues. The protein contains six cysteines whereas phenylalanine and glutamine are absent. The present data, which are the first to be obtained with a phospholipid-transfer protein from a photosynthetic tissue, are compared to the amino acid sequences determined with plant and animal proteins involved in the intracellular transport of hydrophobic compounds.
已确定从菠菜叶中分离出的磷脂转移蛋白的完整氨基酸序列。通过对溴化氰片段和胰蛋白酶消化获得的肽进行高效液相色谱分析，阐明了菠菜蛋白的一级结构。菠菜蛋白的单条多肽链由91个氨基酸残基组成。该蛋白含有6个半胱氨酸，而没有苯丙氨酸和谷氨酰胺。本文首次获得了来自光合组织的磷脂转移蛋白的数据，并与参与疏水性化合物细胞内运输的植物和动物蛋白的氨基酸序列进行了比较。
