Partial characterization of human complement factor H by protein and cDNA sequencing: Homology with other complement and non-complement proteins
- 1 January 1986
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 6 (1) , 65-72
- https://doi.org/10.1007/bf01145180
Abstract
Factor H, a control protein of the human complement system, is closely related in functional activity to two other complement control proteins, C4b-binding protein (C4bp) and complement receptor type 1 (CR1). C4bp is known to have an unusual primary structure consisting of eight homologous units each about 60 amino acids long. Such units also occur in the N-terminal regions of the complement proteins C2 and factor B, and in the non-complement serum glycoprotein β2I. Amino acid sequencing, and sequencing of a factor H cDNA clone, show that factor H also contains internal repeating units, and is homologous to the proteins listed above.Keywords
This publication has 32 references indexed in Scilit:
- Tissue-specific regulation of two functional malic enzyme mRNAs by triiodothyronineBiochemistry, 1985
- Human C3b- and C4b-regulatory proteins: a new multi-gene familyImmunology Today, 1985
- Localization of the Gene Encoding the Human Interleukin-2 Receptor on Chromosome 10Science, 1985
- Amino acid sequence studies of human C4b-binding protein: N-terminal sequence analysis and alignment of the fragments produced by limited proteolysis with chymotrypsin and the peptides produced by cyanogen bromide treatmentMolecular Immunology, 1985
- Expression of complement factor H on the cell surface of the human monocytic cell line U937European Journal of Immunology, 1985
- Molecular cloning of cDNA encoding human interleukin-2 receptorNature, 1984
- TheFactor BandC2genesPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1984
- Isolation of β-globin-related genes from a human cosmid libraryGene, 1981
- Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencingJournal of Molecular Biology, 1980
- Sequence of the amino-terminal 349 residues of rabbit muscle glycogen phosphorylase including the sites of covalent and allosteric controlBiochemistry, 1978