Abstract
The major histocompatibility complex (MHC)-linked fourth component of complement (C4) shows a high degree of polymorphism in several animal species1–4. In man C4 polymorphism was detected by distinct charge differences of the variants5–7. O'Neill et al.8 showed that this C4 polymorphism was controlled by two closely linked genetic loci, F (C4A) and S (C4B) and these results were extended by Awdeh et al.9 with an improved typing method. Biochemical analysis of human C4 has revealed that it consists of three polypeptide chains, α, β and γ10. In all reports so far on the molecular analysis of human C410–13, no molecular weight differences between the A and B locus-encoded molecules have been noticed. Here we demonstrate that the C4A and C4B locus-encoded α-chains have a molecular weight (MW) of 96,000 and 94,000, respectively, presenting for the first time a molecular basis for the difference between all C4A and C4B variants tested. Even rare variants that are difficult to allocate to the A or B locus on the basis of charge differences14,15 could be identified as C4A or C4B variants in this way, thereby providing new insights into the relationships between the C4A and C4B loci.
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Roos, M., Mollenhauer, E., Démant, P. et al. A molecular basis for the two locus model of human complement component C4. Nature 298, 854–856 (1982). https://doi.org/10.1038/298854a0
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DOI: https://doi.org/10.1038/298854a0
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