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- W2415495291 abstract "The isolation of complementary DNA clones for both enzymic subcomponents of C1 has made it possible to derive their complete amino acid sequences and to verify and extend previous protein data. We review here recent advances in studies of the C1r and C1s proteins and of the corresponding genes, using molecular probes. The mosaic structure of these proteins has been compared to the exon-intron organization of the C1s gene. Surprisingly, the C1r and the C1s genes feature an intronless serine protease domain, at variance with all vertebrate serine proteases. Moreover, C1r and C1s are related in evolution to haptoglobin, a serine protease analog lacking enzymic activity. The C1r and C1s genes are closely linked in an unusual tail to tail orientation. These findings are discussed with regard to the apparently coordinate expression of these complement components and to the combined nature of most C1r and C1s deficiencies. We also discuss the implications of the successful production of C1r protein using recombinant DNA technology." @default.
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- W2415495291 date "1989-07-01" @default.
- W2415495291 modified "2023-09-23" @default.
- W2415495291 title "Human complement C1r and C1s proteins and genes: studies with molecular probes." @default.
- W2415495291 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2572213" @default.
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