Open AccessNucleotide sequence of cDNA and derived amino acid sequence of human complement component C9.
Author(s) -
Richard G. DiScipio,
Michael R. Gehring,
Eckhard R. Podack,
Chen Chen Kan,
Tony E. Hugli,
Georg H. Fey
Publication year - 1984
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.81.23.7298
Subject(s) - complementary dna , peptide sequence , nucleic acid sequence , biology , amino acid , biochemistry , oligonucleotide , microbiology and biotechnology , sequence (biology) , protein primary structure , nucleotide , cdna library , transmembrane domain , sequence analysis , gene
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.