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Isolation of Fc receptor shed from pig lymphocytes by a temperature shift
Author(s) -
Vojtíšková Jarmila,
Franěk František
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80455-x
Subject(s) - chromatography , chemistry , affinity chromatography , centrifugation , antibody , receptor , diethylamine , electrophoresis , immunoglobulin g , gel electrophoresis , biochemistry , biology , enzyme , immunology , organic chemistry
Lymphocytes obtained from pig blood by gradient centrifugation were subjected to a temperature shift (4 to 37°C). The proteins released from the plasma membrane were fractionated by affinity chromatography using immunoglobulin G immobilized on fine polyamide particles. The main component liberated from the adsorbent by diethylamine buffer (pH 11.5) exhibited an apparent M r of 18000–20000 in SDS—polyacrylamide gel electrophoresis. This crude receptor preparation possessed a substantially higher affinity to immobilized immunoglobulin G than to immobilized Fab fragment and inhibited significantly the binding of labeled immunoglobulin G to pig lymphocytes.