Isolation of Fc receptor shed from pig lymphocytes by a temperature shift

FEBS Letters

Vojtíšková, Jarmila¹  Franěk, František¹ 

[1] Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Vídeňská 1083, CS-142 20 Praha 4, Czechoslovakia

关键词: Fc receptor;    Pig immunoglobulin;    Proteolytic fragment;    Pig lymphocyte;    Affinity chromatography;    PBS;    phosphate-buffered saline (150 mM NaCl;    20 mM NaH2PO4 buffered to pH 7.4);    IgG;    immunoglobulin G;    Fab;    Fc;    pFc′;    proteolytic fragments of IgG;    BSA;    bovine serum albumin;    PSA;    pig serum albumin;    PMSF;    phenylmethylsulfonyl fluoride;    NP40;    Nonidet P40;   

DOI  :  10.1016/0014-5793(84)80455-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown