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cDNA Clone Spanning the α -γ Subunit Junction in the Precursor of the Murine Fourth Complement Component (C4)

cDNA clones carrying parts of murine fourth complement component (C4, serum substance protein) mRNA sequences have been identified by differential hybridization to mRNA from a high C4-producing strain, B10.WR, and a congeneic low C4 strain, B10.BR, followed by hybrid-selected translation and DNA seq...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1983-08, Vol.80 (16), p.5061-5065
Main Authors: Ogata, R. T., Shreffler, D. C., Sepich, D. S., Lilly, S. P.
Format: Article
Language:English
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Summary:cDNA clones carrying parts of murine fourth complement component (C4, serum substance protein) mRNA sequences have been identified by differential hybridization to mRNA from a high C4-producing strain, B10.WR, and a congeneic low C4 strain, B10.BR, followed by hybrid-selected translation and DNA sequence analysis. One clone, pMLC4/w7-2, encodes an open amino acid reading frame that includes four tandem arginine residues immediately preceding a sequence 85% homologous with the NH2-terminal sequence of the human C4 γ -chain. The amino acid composition of the predicted sequence upstream of the tandem arginines matches quite closely with the composition of a similar sized peptide at the COOH terminus of the human C4 α chain. The latter result raises questions regarding the nature and extent of plasma-mediated postsynthetic processing of the C4 α -chain COOH terminus. The results also demonstrate that strain differences in plasma C4 levels (low C4 vs. high C4) reflect differences in steady-state levels of liver C4 mRNA in these strains.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.80.16.5061