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In this study, Fc gamma-receptors were isolated from normal human peripheral blood lymphocytes by prolonged incubation at 37 degrees C and purified by affinity chromatography using Sepharose 4B combined with heat-aggregated IgG. These labile Fc gamma R-receptors were shown to be functionally active with an apparent molecular weight of 60 K. Serum Fc gamma-receptor like molecules were also isolated and were shown to be of similar molecular weight. In addition, a high molecular weight (greater than 19S) serum IgG-binding protein was found. The basic sub-unit structure of this molecule was also 60K suggesting that the Fc gamma-receptor may exist in a polymeric or complexed form in normal human serum.
G P Sandilands, and
M G Peel, and
R N MacSween
March 1987,
Immunology,
G P Sandilands, and
M G Peel, and
R N MacSween
January 1984,
Survey of immunologic research,
G P Sandilands, and
M G Peel, and
R N MacSween
January 1984,
International archives of allergy and applied immunology,
G P Sandilands, and
M G Peel, and
R N MacSween
February 1980,
Biomedicine / [publiee pour l'A.A.I.C.I.G.],
G P Sandilands, and
M G Peel, and
R N MacSween
October 1979,
Clinical immunology and immunopathology,
G P Sandilands, and
M G Peel, and
R N MacSween
August 1984,
Cryobiology,
G P Sandilands, and
M G Peel, and
R N MacSween
December 1980,
Biochemistry,
G P Sandilands, and
M G Peel, and
R N MacSween
January 1979,
Scandinavian journal of immunology,
G P Sandilands, and
M G Peel, and
R N MacSween
September 1976,
Journal of immunology (Baltimore, Md. : 1950),
G P Sandilands, and
M G Peel, and
R N MacSween
April 1977,
Clinical and experimental immunology,
