兔血红蛋白的生物合成：利用人血红蛋白链研究分子组装

Rabbit hemoglobin biosynthesis: use of human hemoglobin chains to study molecule completion.

作者信息

Shaeffer J R, Trostle P K, Evans R F

出版信息

Science. 1967 Oct 27;158(3800):488-90. doi: 10.1126/science.158.3800.488.

DOI:10.1126/science.158.3800.488

Abstract

A cell-free protein-synthesizing system made from rabbit reticulocytes was used to incorporate (14)C-amino acids into hemoglobin. Electrophoretic analyses of the soluble products of this cell-free system revealed a fraction containing rabbit (14)C-alpha chains in addition to the rabbit (14)C-hemoglobin. The addition of isolated human hemoglobin beta chains to this system during active synthesis inhibited the release of newly synthesized rabbit (14)C-beta chains into solution from the ribosome fraction. This inhibition was possibly a result of hybrid hemoglobin formation between rabbit alpha and human beta chains. A model of hemoglobin construction in which soluble alpha chains are intermediates is suggested. These alpha chains may aid in the release of beta chains from the polyribosomes during the completion of the hemoglobin molecule.

摘要

用兔网织红细胞制成的无细胞蛋白质合成系统，将（14）C-氨基酸掺入血红蛋白中。对该无细胞系统的可溶性产物进行电泳分析发现，除了兔（14）C-血红蛋白外，还有一个含有兔（14）C-α链的组分。在活性合成过程中，向该系统中添加分离的人血红蛋白β链，抑制了新合成的兔（14）C-β链从核糖体组分释放到溶液中。这种抑制可能是兔α链和人β链之间形成杂种血红蛋白的结果。提出了一种血红蛋白构建模型，其中可溶性α链是中间体。这些α链可能有助于在血红蛋白分子完成过程中，β链从多核糖体中释放出来。