Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.

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Standard

Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens. / Eriksson, H; Nissen, Mogens Holst.

In: Biochemical and Biophysical Research Communications, Vol. 187, No. 2, 1992, p. 832-8.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Eriksson, H & Nissen, MH 1992, 'Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.', Biochemical and Biophysical Research Communications, vol. 187, no. 2, pp. 832-8.

APA

Eriksson, H., & Nissen, M. H. (1992). Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens. Biochemical and Biophysical Research Communications, 187(2), 832-8.

Vancouver

Eriksson H, Nissen MH. Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens. Biochemical and Biophysical Research Communications. 1992;187(2):832-8.

Author

Eriksson, H ; Nissen, Mogens Holst. / Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens. In: Biochemical and Biophysical Research Communications. 1992 ; Vol. 187, No. 2. pp. 832-8.

Bibtex

@article{94e84a60ba3411ddae57000ea68e967b,
title = "Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.",
abstract = "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.",
author = "H Eriksson and Nissen, {Mogens Holst}",
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",
year = "1992",
language = "English",
volume = "187",
pages = "832--8",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.

AU - Eriksson, H

AU - Nissen, Mogens Holst

N1 - 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

PY - 1992

Y1 - 1992

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 1530639

VL - 187

SP - 832

EP - 838

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

ID: 8746698