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Isolation of tryptic fragments of human C4 expressing Chido and Rodgers antigens

Lundwall, Åke LU ; Hellman, U.; Eggertsen, G. and Sjöquist, J. (1982) In Mol Immunol 19(2). p.1655-65
Abstract
It has been shown previously that methylamine is incorporated into the alpha-chain of human C4, resulting in a loss of haemolytic function and the appearance of a free thiol group in the molecule. In the present study it was demonstrated that a fragment resembling C4d is liberated from C4 by trypsin. The fragment--Try-C4d--contains both the methylamine binding site and the free thiol group. When separated on DEAE-Sepharose, four types of Try-C4d, differing in charge and size, could be defined. The size difference was found to parallel the presence of Chido and Rodgers blood group antigens. Fragments of Mr 30,000 carried the Rodgers antigen and the Chido antigen was expressed on fragments of Mr 28,000.
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Contribution to journal
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published
subject
keywords
Isoantigens/*analysis, Humans, Electrophoresis, Polyacrylamide Gel, Complement C4/*immunology/isolation & purification/metabolism, Gel, DEAE-Cellulose, Chromatography, Amino Acid Sequence, Amino Acids/analysis, Methylamines/metabolism, Molecular Weight, Peptide Fragments/*immunology/isolation & purification, Research Support, Non-U.S. Gov't, Sulfhydryl Compounds/metabolism, Trypsin
in
Mol Immunol
volume
19
issue
2
pages
1655 - 65
external identifiers
  • Scopus:0020411227
language
English
LU publication?
no
id
53ee42dc-a895-4d86-bafc-555fe59eaab2 (old id 3965029)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7162521
date added to LUP
2013-08-11 18:36:12
date last changed
2016-06-29 09:17:46
@misc{53ee42dc-a895-4d86-bafc-555fe59eaab2,
  abstract     = {It has been shown previously that methylamine is incorporated into the alpha-chain of human C4, resulting in a loss of haemolytic function and the appearance of a free thiol group in the molecule. In the present study it was demonstrated that a fragment resembling C4d is liberated from C4 by trypsin. The fragment--Try-C4d--contains both the methylamine binding site and the free thiol group. When separated on DEAE-Sepharose, four types of Try-C4d, differing in charge and size, could be defined. The size difference was found to parallel the presence of Chido and Rodgers blood group antigens. Fragments of Mr 30,000 carried the Rodgers antigen and the Chido antigen was expressed on fragments of Mr 28,000.},
  author       = {Lundwall, Åke and Hellman, U. and Eggertsen, G. and Sjöquist, J.},
  keyword      = {Isoantigens/*analysis,Humans,Electrophoresis,Polyacrylamide Gel,Complement C4/*immunology/isolation & purification/metabolism,Gel,DEAE-Cellulose,Chromatography,Amino Acid Sequence,Amino Acids/analysis,Methylamines/metabolism,Molecular Weight,Peptide Fragments/*immunology/isolation & purification,Research Support,Non-U.S. Gov't,Sulfhydryl Compounds/metabolism,Trypsin},
  language     = {eng},
  number       = {2},
  pages        = {1655--65},
  series       = {Mol Immunol},
  title        = {Isolation of tryptic fragments of human C4 expressing Chido and Rodgers antigens},
  volume       = {19},
  year         = {1982},
}