An improved method for refolding recombinant decay accelerating factor for therapeutic studies.
Decay accelerating factor (DAF) is a very potent complement regulatory protein which holds promise for clinical usage. Here we report on an improved procedure for refolding both rat and human DAF over-expressed in Escherichia coli. It was shown that 50-70% of the inclusion body could be refolded to soluble active protein. This method excludes the use of L-arginine, which is expensive, and can be used to prepare a large quantity of recombinant DAF for therapeutic studies.
Xu
Jiang
J
Department of Neurology, Tangdu Hospital, The Fourth Military Medical University, Xi'An, China.
Hu
Yongliang
Y
Gong
Meiliang
M
Sun
Chenjing
C
Xu
Zhikai
Z
Li
Zhuyi
Z
Wu
Xingan
X
D000818:Animals; D001120:Arginine / Q000737:chemistry; D018958:CD55 Antigens / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000627:therapeutic use; D003001:Cloning, Molecular; D006367:HeLa Cells; D006801:Humans; D002479:Inclusion Bodies / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D020673:Protein Renaturation; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000627:therapeutic use
D018958:CD55 Antigens; D011993:Recombinant Fusion Proteins; D001120:Arginine