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Hereditary subtypic patterns detected in the Ba fragment of complement factor B: Occurrence of four common alleles in Japanese
Author(s) -
Suzuki Koichi,
Ito Shigenori,
Tamura Akiyoshi,
Fujita Kiyoshi,
Matsumoto Hideo
Publication year - 1990
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150111011
Subject(s) - allele , fragment (logic) , genetics , biology , complement (music) , complement factor b , factor h , microbiology and biotechnology , complement system , phenotype , antibody , gene , mathematics , algorithm , complementation
A procedure which can detect subtype‐specific minor bands of factor B (BF) by polyacrylamide gel isoelectric focusing is presented. After zymosan‐mediated fragmentation of BF in serum via alternative pathway for complement activation, serum samples are subjected to isoelectric focusing in a narrow pH range (4.2–4.9). The Ba fragments are detected by using immunoblotting. In addition to the previously reported minor bands with subtypic specificities, heterogeneities are observed in other minor band group, where a single minor band corresponds exclusively to a subtype in a regular combination with the previously announced subtypic patterns. A one‐to‐one correspondence of a single band to each subtype provides an unambiguous determination for three subtypic phenotypes deduced from the two divided BF*F alleles, BF*FA and BF*FB. An autosomal codominant heredity is confirmed through segregation analysis. A population survey reveals that four common alleles, BF*S, BF*FA, BF*FB, BF*Fb1, occur in a Japanese population and the former three alleles, except BF*Fb1, occur in a Cambodian population. The presence or absence of a single anodal minor band was found to be the only difference after neuraminidase treatment of FA and FB, implying that an amino acid substitution responsible for the FA–FB subtypic difference is involved in an additional acquisition in FA of an oligosaccharide unit with a charged sialic acid.