Farchaus J, Dilley R A
Arch Biochem Biophys. 1986 Jan;244(1):94-101. doi: 10.1016/0003-9861(86)90097-4.
The Mr 10,000 phosphoprotein was purified from photosystem II particles by solubilization of the particles in 5% (w/v) dodecyl dimethylamine oxide, centrifugation in 10% (w/v) sucrose, and three chromatography steps. The purified phosphoprotein showed a unique NH2 terminus indicating a highly purified polypeptide. The amino acid sequence for the first nine residues is NH2-Ala-Thr-Gln-Thr-Val-Glu-Ser-Ser-Ser . . . COOH. The amino acid composition was determined and could also be used to help distinguish the polypeptide from other known thylakoid proteins. The sequence and composition data indicated that the Mr 10,000 phosphoprotein is neither the hydrophobic 8-kDa subunit of the energy coupling complex nor cytochrome b-559, but rather a unique, as yet unidentified, polypeptide associated with photosystem II.
通过用5%（w/v）十二烷基二甲基氧化胺溶解光系统II颗粒、在10%（w/v）蔗糖中离心以及三步色谱法，从光系统II颗粒中纯化出了分子量为10,000的磷蛋白。纯化后的磷蛋白显示出独特的氨基末端，表明其为高度纯化的多肽。前九个残基的氨基酸序列为NH2 - 丙氨酸 - 苏氨酸 - 谷氨酰胺 - 苏氨酸 - 缬氨酸 - 谷氨酸 - 丝氨酸 - 丝氨酸 - 丝氨酸……COOH。测定了氨基酸组成，其也可用于帮助将该多肽与其他已知的类囊体蛋白区分开来。序列和组成数据表明，分子量为10,000的磷蛋白既不是能量偶联复合物的疏水8 kDa亚基，也不是细胞色素b - 559，而是与光系统II相关的一种独特的、尚未鉴定的多肽。
