DiScipio R G, Gehring M R, Podack E R, Kan C C, Hugli T E, Fey G H
Proc Natl Acad Sci U S A. 1984 Dec;81(23):7298-302. doi: 10.1073/pnas.81.23.7298.
The nucleotide sequence coding for the ninth component of human complement (C9) has been determined and the corresponding amino acid sequence has been derived. A human liver cDNA library was screened by the colony-hybridization technique using two radiolabeled oligonucleotide probes that correspond to known regions of the C9 amino acid sequence. Two recombinant plasmids were isolated and their cDNA inserts were sequenced. The derived protein sequence consists of 537 amino acids in a single polypeptide chain. A profile of the hydropathic index versus sequence number indicates that the amino-terminal half of C9 is predominantly hydrophilic in character whereas the carboxyl-terminal section of this protein is more hydrophobic. The amphipathic organization of the primary structure of C9 is consistent with the known potential of polymerized C9 to penetrate lipid bilayers, causing the formation of transmembrane channels.
编码人补体第九成分(C9)的核苷酸序列已被确定,相应的氨基酸序列也已推导出来。利用两种与C9氨基酸序列已知区域相对应的放射性标记寡核苷酸探针,通过菌落杂交技术筛选人肝脏cDNA文库。分离出两个重组质粒,并对其cDNA插入片段进行测序。推导得到的蛋白质序列由一条单多肽链中的537个氨基酸组成。亲水性指数与序列数的分布图表明,C9的氨基末端一半主要具有亲水性,而该蛋白质的羧基末端部分则更具疏水性。C9一级结构的两亲性组织与已知的聚合C9穿透脂质双层、导致形成跨膜通道的潜力一致。