Literature DB >> 3492559

High resolution electrophoresis for the allotyping of human C4. Proposal of a relational nomenclature.

K Kölble, V Rukavina, J R Kalden.   

Abstract

Among the major histocompatibility complex (MHC)-linked complement genes, the loci for C4A and C4B exhibit the most extensive structural polymorphisms. Therefore the differentiation of variant and complex C4 phenotypes often proves difficult in conventional immunofixation electrophoresis. To improve the available technique of C4 typing a closed horizontal electrophoresis system was combined with poly- and monoclonal alkaline phosphatase immunoprobing on contact diffusion blots. The high resolution and sensitivity of this method not only facilitated C4 allotyping but also revealed additional polymorphic variation. Relative electrophoretic mobilities specific for each C4 allotype were established by computerized remission densitometry and provided the basis for a quantitative denomination of C4 variants. Typing by high resolution electrophoresis and the proposed relational C4 nomenclature could be valuable for further immunogenetical studies of the C4 protein polymorphism.

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Year:  1987        PMID: 3492559     DOI: 10.1016/0022-1759(87)90369-3

Source DB:  PubMed          Journal:  J Immunol Methods        ISSN: 0022-1759            Impact factor:   2.303


  2 in total

1.  Structure and homology of human C1q receptor (collectin receptor).

Authors:  R Malhotra; A C Willis; J C Jensenius; J Jackson; R B Sim
Journal:  Immunology       Date:  1993-03       Impact factor: 7.397

2.  A calreticulin-like protein co-purifies with a '60 kD' component of Ro/SSA, but is not recognized by antibodies in Sjögren's syndrome sera.

Authors:  J Lu; A C Willis; R B Sim
Journal:  Clin Exp Immunol       Date:  1993-12       Impact factor: 4.330

  2 in total

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