Purification and characterization of cyclosporine and FK-506 binding proteins from a human T-helper cell line.
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.
Palaszynski
E W
EW
Department of Laboratory Medicine, Children's National Medical Center, Washington, DC 20010-2970.
Donnelly
J G
JG
Soldin
S J
SJ
D000591:Amino Acid Isomerases / Q000737:chemistry / Q000302:isolation & purification*; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002460:Cell Line; D002853:Chromatography, Liquid; D003524:Cyclosporins / Q000378:metabolism*; D003600:Cytosol / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008970:Molecular Weight; D019696:Peptidylprolyl Isomerase; D011869:Radioligand Assay; D006377:T-Lymphocytes, Helper-Inducer / Q000737:chemistry*; D016559:Tacrolimus
D000900:Anti-Bacterial Agents; D002352:Carrier Proteins; D003524:Cyclosporins; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase; D016559:Tacrolimus