Isolation of tryptic fragments of human C4 expressing Chido and Rodgers antigens
(1982) In Mol Immunol 19(2). p.65-1655- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3965029
- author
- Lundwall, Åke LU ; Hellman, U. ; Eggertsen, G. and Sjöquist, J.
- publishing date
- 1982
- type
- Contribution to journal
- publication status
- 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
- 65 - 1655
- external identifiers
-
- scopus:0020411227
- language
- English
- LU publication?
- no
- additional info
- 12
- 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
- 2016-04-04 13:43:40
- date last changed
- 2021-01-03 10:12:56
@article{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.}}, 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}}, language = {{eng}}, number = {{2}}, pages = {{65--1655}}, series = {{Mol Immunol}}, title = {{Isolation of tryptic fragments of human C4 expressing Chido and Rodgers antigens}}, url = {{http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7162521}}, volume = {{19}}, year = {{1982}}, }