Gambacurta A, Piro M C, Ascoli F
Department of Experimental Medicine and Biochemical Sciences, Tor Vergata University, Rome, Italy.
FEBS Lett. 1993 Sep 6;330(1):90-4. doi: 10.1016/0014-5793(93)80926-l.
The overexpression of the fully functional, cooperative homodimeric hemoglobin of the bivalve mollusc, Scapharca inaequivalvis, has been accomplished in E. coli from its cDNA. The latter was isolated by PCR amplification of total RNA and sequenced. The cDNA-derived sequence differed by a single amino acid when compared to that previously obtained from purified protein. Interest in this hemoglobin resides in the unique assemblage of the two identical subunits, with the heme groups facing each other in the inside of the molecule, opposite to that occurring in vertebrate hemoglobins. The results presented here are the basis for future studies of structure/function relationships by site directed mutagenesis.
双壳贝类不等齿毛蚶（Scapharca inaequivalvis）完全功能性、协同性同型二聚体血红蛋白在大肠杆菌中通过其cDNA实现了过表达。后者通过对总RNA进行PCR扩增分离得到并测序。与之前从纯化蛋白获得的序列相比，cDNA衍生序列仅有一个氨基酸不同。对这种血红蛋白的兴趣在于两个相同亚基的独特组装方式，血红素基团在分子内部彼此相对，这与脊椎动物血红蛋白的情况相反。本文给出的结果是未来通过定点诱变研究结构/功能关系的基础。
