Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.
Research output: Contribution to journal › Journal article › Research › peer-review
Apart from cleaving C1s, we demonstrate for the first time that: 1) at concentrations found in serum, the activated forms of the complement components C1r in addition to C1s can cleave the heavy chain of MHC class I antigens, 2) the cleavage by C1r and C1s is seemingly dependent upon a native configuration of the MHC class I antigen, since heat denaturation of the HLA antigens reduce the cleavage. The proteolytic fragments following C1 cleavage were characterized by precipitation with Con A-Sepharose, anti-MHC class I and anti-beta 2-microglobulin antibodies. The proteolysis of the alpha-chain of MHC class I was shown to take place between the alpha 2- and alpha 3- domains as estimated by the Con A-Sepharose precipitation pattern on SDS-PAGE. The alpha 1/alpha 2 fragment was still shown to interact with beta 2-microglobulin as shown by immunoprecipitation.
Original language | English |
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Journal | Biochemical and Biophysical Research Communications |
Volume | 187 |
Issue number | 2 |
Pages (from-to) | 832-8 |
Number of pages | 6 |
ISSN | 0006-291X |
Publication status | Published - 1992 |
Bibliographical note
Keywords: Antibodies, Monoclonal; Cell Line; Complement C1r; Complement C1s; Electrophoresis, Polyacrylamide Gel; Glycosylation; Heat; Histocompatibility Antigens Class I; Humans; Immunosorbent Techniques; Molecular Weight; Peptide Fragments; Protein Conformation; Protein Denaturation; Structure-Activity Relationship
ID: 8746698