[Expression, purification and characterization of recombinant human cyclophilin A].
Plasmid-derived expression of the human CyPA in E. coli would make it possible to obtain ample protein quantities and to avoid difficult task of obtaining human tissues for protein purification. The cDNA encoding human CyPA from MT4 lymph cell line has been cloned and an expression vector (pET11/CyPA) has been constructed under control of the T7 promoter for efficient expression in E. coli. The recombinant CyPA is produced at 41% of total soluble cell protein, and showed the peptidyl-prodyl cis-trans isomerase activity.
Li
F
F
Center of Medical Laboratory Sciences of PLA, Jinling Hospital, Nanjing 210002.
Zhao
Q
Q
Wu
J
J
Shan
X
X
D002460:Cell Line; D021984:Cyclophilin A / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D019696:Peptidylprolyl Isomerase / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D019745:cis-trans-Isomerases / Q000378:metabolism
D011994:Recombinant Proteins; D019745:cis-trans-Isomerases; D021984:Cyclophilin A; D019696:Peptidylprolyl Isomerase