Sequence analysis of a cDNA clone encoding the C-terminal end of human complement factor H
- 1 March 1987
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 7 (3) , 201-207
- https://doi.org/10.1007/bf01124790
Abstract
Peptide sequencing of the complement system regulatory protein, factor H, permitted the synthesis of a mixed sequence oligonucleotide probe. Human liver cDNA libraries were screened and factor H-specific clones selected. No full-length clone was obtained, but the largest available clone, R2a, was found to encode the C-terminal 657 amino acids of factor H. The derived amino acid sequence consists of 10 contiguous internally homologous segments, each about 60 amino acids long. Sequences homologous to these are found in several other complement and non-complement proteins. Such sequences are likely to represent a particular type of tertiary structure subunit.This publication has 21 references indexed in Scilit:
- Structure and specificity of complement receptorsImmunology Letters, 1987
- Cloning of decay-accelerating factor suggests novel use of splicing to generate two proteinsNature, 1987
- Quantitative variations of the C3b/C4b receptor (CR1) in human erythrocytes are controlled by genes within the regulator of complement activation (RCA) gene cluster.The Journal of Experimental Medicine, 1986
- Complement system proteins which interact with C3b or C4b A superfamily of structurally related proteinsImmunology Today, 1986
- Human complement factor H: isolation of cDNA clones and partial cDNA sequence of the 38‐kDa tryptic fragment containing the binding site for C3bEuropean Journal of Immunology, 1986
- Partial characterization of human complement factor H by protein and cDNA sequencing: Homology with other complement and non-complement proteinsBioscience Reports, 1986
- Human C3b- and C4b-regulatory proteins: a new multi-gene familyImmunology Today, 1985
- Expression of complement factor H on the cell surface of the human monocytic cell line U937European Journal of Immunology, 1985
- The structural basis of the multiple forms of human complement component C4Cell, 1984
- Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase IJournal of Molecular Biology, 1977