Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q
| العنوان: | Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q |
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| المؤلفون: | Derek J. Blake, G. C. Sellar, Kenneth B.M. Reid |
| المصدر: | Biochemical Journal. 274:481-490 |
| بيانات النشر: | Portland Press Ltd., 1991. |
| سنة النشر: | 1991 |
| مصطلحات موضوعية: | Macromolecular Substances, Molecular Sequence Data, Restriction Mapping, Sequence alignment, Biology, Biochemistry, Monocytes, Mice, Sequence Homology, Nucleic Acid, Complementary DNA, Animals, Humans, Coding region, Amino Acid Sequence, Cloning, Molecular, Molecular Biology, Gene, Complement C1q, Peptide sequence, Gene Library, Genetics, Base Sequence, Nucleic acid sequence, DNA, Cell Biology, Blotting, Northern, Cosmids, Molecular biology, Blotting, Southern, Genes, C1q domain, RNA, Collagen, Research Article |
| الوصف: | A partial cDNA clone for the A-chain of human complement subcomponent C1q was isolated from a monocyte library. Use of the A-chain cDNA clone, and a previously characterized B-chain cDNA clone [Reid (1985) Biochem. J. 231, 729-735] allowed the isolation of overlapping cosmid clones that were shown to contain the genes encoding the A-, B- and C-chains of human C1q. The three genes were found to be aligned, 5′→3′, in the same orientation, in the order A-C-B on a 24 kb stretch of DNA on chromosome 1p. The A-, B- and C-chain genes are approx. 2.5, 2.6 and 3.2 kb long respectively, and each contains one intron, located within a codon for a glycine residue found half-way along the collagen-like region present in each chain. These glycine residues are located just before the point where the triple-helical portions of the C1q molecule appear to bend when viewed in the electron microscope. Southern-blot analyses indicated that there is only one gene per chain, and preliminary examination of genomic DNA from several C1q-deficient patients showed no evidence for major deletions or insertions within the A-, B- or C-chain genes. The DNA sequence of the coding region of the C-chain gene allows the completion of the entire derived amino acid sequence for the human C1q molecule. The globular, C-terminal, regions of the chains of C1q show a strong similarity in amino acid sequence to the non-collagen-like, C-terminal, regions of the type VIII and type X collagens, indicating structural and evolutionary relationships between these three molecules. |
| تدمد: | 1470-8728 0264-6021 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7aab228fc461c6835fc5d8be0ad95f88Test https://doi.org/10.1042/bj2740481Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....7aab228fc461c6835fc5d8be0ad95f88 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14708728 02646021 |
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