叶绿体核糖体蛋白的纯化、一级结构和同源关系。

Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Ihnestrasse 63-73, D-1000 Berlin 33, Germany.

Proc Natl Acad Sci U S A. 1982 Nov;79(22):6871-5. doi: 10.1073/pnas.79.22.6871.

A chloroplast ribosomal protein that showed immunological homology to Escherichia coli ribosomal protein L12 was purified from spinach (Spinacia oleracea) leaves and its primary structure was determined by manual micro Edman degradation. The protein is composed of 130 amino acid residues and has M(r) 13,576. It shows structural features characteristic of the L12 proteins of eubacterial 70S ribosomes (e.g., identical amino acid residues in about 50% of the sequence) but no apparent homology to the L12-type proteins of eukaryotic cytoplasmic 80S ribosomes. The homology to eubacterial proteins is highest in the COOH-terminal region (70%) and low in the NH(2)-terminal region (<20%).

从菠菜（Spinacia oleracea）叶中纯化出一种与大肠杆菌核糖体蛋白 L12 具有免疫同源性的叶绿体核糖体蛋白，并通过手动微埃德曼降解法测定其一级结构。该蛋白由 130 个氨基酸残基组成，分子量为 13576。它表现出真核生物细胞质 80S 核糖体 L12 型蛋白的结构特征（例如，序列中约 50%的氨基酸残基相同），但与真核生物细胞质 80S 核糖体 L12 型蛋白没有明显的同源性。与真细菌蛋白的同源性在羧基末端区域（70%）最高，在氨基末端区域（<20%）较低。