Polymorphism of human complement component C4
β Scribed by K. Tertia Belt; C. Yung Yu; Michael C. Carroll; Rodney R. Porter
- Publisher
- Springer-Verlag
- Year
- 1985
- Tongue
- English
- Weight
- 499 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0093-7711
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β¦ Synopsis
An assessment has been made of the polymorphism of human complement component C4 by comparing derived amino acid sequences of cDNA and genomic DNA with limited amino acid sequences. In all, one complete and six partial sequences have been obtained from material from three individuals and include two C4A and two C4B alleles. Differences were found between the 4 alleles from 2 loci in only 15 of the 1722 amino acid residues, and 12 lie within one section of 230 residues, which in 1 allele also contains a 3-residue deletion. In three variable positions, an allelic difference in one C4 type was common to the other types. Three nucleotide differences were found in four introns. In spite of marked differences in their chemical reactivity, the many allelic forms appear to differ in less than 17o of their amino acid residue positions. This unusual pattern of polymorphism may be due to recent duplication of the C4 gene, or may have arisen by selection as a result of the biological role of C4, which interacts in the complement sequence with nine other proteins necessitating conservation of much of the surface structure.
π SIMILAR VOLUMES
Proteins were separated by prolonged isoelectric focusing in polyacrylamide gels, whereupon C2 bands were detected by a specific hemolytic assay. This was performed by treating the gel with iodine to increase C2 activity, and then developing C2 bands with an agarose gel overlay containing sensitized
C4, one of the early components of the classical complement pathway, is encoded within the class III region of the major histocompatibility complex of man at two highly polymorphic loci, C4A and C4B. Widespread use of C4 typing is, however, hindered by the lack of objective standardized methods. Ob