J. Biol. Chem., Vol. 264, Issue 17, 9780-9784, 06, 1989
Isolation and identification of trophoblast lymphocyte cross-reactive (TLX) antigens from human lymphocytes
IC Kim
Division of Biomedical Research, Lovelace Medical Foundation, Albuquerque, New Mexico 87108.
It has been proposed that allotypic trophoblast lymphocyte cross- reactive
(TLX) antigens are involved in the maintenance of normal human
reproduction. Despite such a potentially important role for TLX antigens,
isolation of human TLX proteins has not yet been reported. As an initial
step toward elucidation of the structure and function of TLX antigens, we
have isolated TLX proteins from Lubrol-solubilized lymphocytes (termed
"wTLX") by anti-trophoblast membrane-Sepharose immunoaffinity
chromatography. Using Ouchterlony immunodiffusion and
immunoelectrophoresis, we have identified an immunoreactive wTLX antigen
which forms a single immunoprecipitation line against absorbed
anti-trophoblast membrane. From 17.5% sodium dodecyl sulfate-
polyacrylamide gel electrophoresis and immunoblot analyses, a 35-kDa band
was determined to be a major protein band in the immunoaffinity- isolated
wTLX fraction, along with multiple minor wTLX bands. These results suggest
the possible existence of antigenic polymorphism of TLX, with predominant
expression of the 35-kDa wTLX antigen in lymphocytes. The strong staining
of the TLX antigens with Coomassie Brilliant Blue and Amido Black indicates
they are largely proteins. Co- isolation of beta 2-microglobulin in the
immunoaffinity-isolated wTLX pool could imply that the wTLX antigens may be
unique class I HLA-like antigens. This possibility has yet to be resolved.
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