Sundelin J, Melhus H, Das S, Eriksson U, Lind P, Trägårdh L, Peterson P A, Rask L
J Biol Chem. 1985 May 25;260(10):6481-7.
The primary structures of rabbit and rat prealbumin have been determined. The amino acid sequence of rabbit prealbumin was determined by analyses of peptides obtained by trypsin and Staphylococcus aureus protease digestions. The rat prealbumin sequence was deduced by analyses of tryptic peptides as well as by nucleotide sequencing of cDNA clones. Both amino acid sequences contain 127 amino acid residues, the same as human prealbumin. Pairwise comparisons show that the three sequences are more than 80% identical. All three prealbumins were found to display significant sequence homology with human thyroxine-binding globulin. A comparison of the primary structures of the prealbumins with the tertiary structure of human prealbumin shows that amino acid replacements are preferentially located at the surface of the molecule and in the loops connecting the beta-strands. The locations of the replacements are discussed as regards the different molecular interactions in which prealbumin is involved.
已确定兔和大鼠前白蛋白的一级结构。兔前白蛋白的氨基酸序列是通过对胰蛋白酶和金黄色葡萄球菌蛋白酶消化产生的肽段进行分析来确定的。大鼠前白蛋白序列是通过对胰蛋白酶肽段的分析以及对cDNA克隆的核苷酸测序推导出来的。两种氨基酸序列均包含127个氨基酸残基，与人类前白蛋白相同。两两比较表明，这三种序列的同源性超过80%。发现所有三种前白蛋白与人甲状腺素结合球蛋白都有显著的序列同源性。将前白蛋白的一级结构与人类前白蛋白的三级结构进行比较表明，氨基酸替换优先位于分子表面以及连接β链的环中。针对前白蛋白所涉及的不同分子相互作用，对替换位置进行了讨论。
