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Reactivity of a Rabbit Antiserum against Highly Purified HLA‐DR Antigens
Author(s) -
KLARESKOG L.,
TRÄGÅRDH L.,
LINDBLOM J. B.,
PETERSON P. A.
Publication year - 1978
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1978.tb00444.x
Subject(s) - antiserum , antigen , microbiology and biotechnology , cytotoxic t cell , glycoprotein , chemistry , biology , immunology , biochemistry , in vitro
A rabbit antiserum has been raised against highly purified, detergent‐Solubilized HLA‐DR antigens. Externally or Internally labelled surface glycoprotein from B‐lymphocytes, epidermis, macrophages, and B‐lymphoma cell lines reacted with the antiserum which precipitated polypeptide chains with the molecular weights 28.000 and 34.000 Such polypeptide chains were not observed when the antiserum was reacted with T‐lymphocytes, T‐cell lymphoma lines, kidney, brain. thymus and spermatozoa. Fab‐fragments of the antiserum completely abolished the cytotoxic action of HLA‐DR alloantisera but had no effect on the cytotoxicity mediated by HLA‐A, B and C loci antisera Moreover, the rabbit antiserum reacted with the same molecules as the HLA‐DR alloantisera. Fab‐fragments of the rabbit antiserum completely abolished the MLR response and from the kinetics of the inhibition it is concluded that the Fab‐fragments may interfere primarily with the initial recognition phase of the MLR.