PURIFICATION AND CHARACTERIZATION OF CYCLOSPORINE AND FK-506 BINDING-PROTEINS FROM A HUMAN T-HELPER CELL-LINE

被引：19
|
作者：
PALASZYNSKI, EW
DONNELLY, JG
SOLDIN, SJ
机构：
[1] CHILDRENS HOSP,NATL MED CTR,DEPT LAB MED,111 MICHIGAN AVE NW,WASHINGTON,DC 20010
[2] GEORGE WASHINGTON UNIV,SCH MED,DEPT BIOCHEM,WASHINGTON,DC 20052
[3] GEORGE WASHINGTON UNIV,SCH MED,DEPT PATHOL,WASHINGTON,DC 20052
[4] GEORGE WASHINGTON UNIV,SCH MED,DEPT PHARMACOL,WASHINGTON,DC 20052
[5] GEORGE WASHINGTON UNIV,SCH MED,DEPT PEDIAT,WASHINGTON,DC 20052
来源：
CLINICAL BIOCHEMISTRY | 1991年 / 24卷 / 01期
关键词：
CYCLOSPORINE; FK-506 BINDING PROTEIN; PROTEIN PURIFICATION; IMMUNE SUPPRESSION; MECHANISM OF ACTION;
D O I：
10.1016/0009-9120(91)90252-A
中图分类号：
R446 [实验室诊断]; R-33 [实验医学、医学实验];
学科分类号：
1001 ;
摘要：
Cytosolic proteins that specifically bind cyclosporine A and FK-506 were isolated and purified from the JURKAT human T-helper cell line. These binding proteins were purified by affinity, molecular weight exclusion and weak cation exchange column chromatography. Radiolabeled cyclosporine A specifically bound to a approximately 17 kDa molecule which is cyclophilin and also bound to a approximately 50 kDa protein(s). Radiolabeled FK-506 did not bind to the approximately 17 kDa molecular weight protein, but specifically bound to soluble approximately 10 kDa and approximately 50 kDa proteins.
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页码：63 / 70
页数：8
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