COOPERATIVE HOMODIMERIC HEMOGLOBIN FROM SCAPHARCA-INAEQUIVALVIS - CDNA CLONING AND EXPRESSION OF THE FULLY FUNCTIONAL PROTEIN IN ESCHERICHIA-COLI
COOPERATIVE HOMODIMERIC HEMOGLOBIN FROM SCAPHARCA-INAEQUIVALVIS - CDNA CLONING AND EXPRESSION OF THE FULLY FUNCTIONAL PROTEIN IN ESCHERICHIA-COLI
复制标题
DOI：
10.1016/0014-5793(93)80926-l
复制
发表时间：
1993-09-06
期刊：
影响因子：
3.5
通讯作者：
ASCOLI, F
中科院分区：
文献类型：
--
作者：
GAMBACURTA, A;PIRO, MC;ASCOLI, F
双壳类软体动物Scapharca inaequvalvis的功能齐全、相互协作的同源二聚体血红蛋白在大肠杆菌中的高效表达是从其基因序列中获得的。后者通过总RNA的聚合酶链式反应(PCR)扩增分离并测序。与以前从纯化蛋白中获得的序列相比，该序列只有一个氨基酸不同。对这种血红蛋白的兴趣在于两个相同亚基的独特组合，在分子内部，血红素基团相互面对，与脊椎动物血红蛋白中的亚基相反。本研究结果为进一步通过定点突变研究结构/功能关系奠定了基础。
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.