The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions.
The complete cDNA encoding human thiol-specific antioxidant protein (PRP) was isolated from a human brain cDNA library in the lambda Zap expression vector. An open reading frame (ORF) was identified and found to encode a polypeptide of 197 aa with a M(r) of 21,729. The cDNA contained 98 bp of 5'-untranslated sequence (UTR) and 259 bp of 3'-UTR containing a poly(A) signal, AATAAA. Expression of the human PRP cDNA in Escherichia coli yielded a functionally active protein. The observed local sequence homologies between human PRP and other homologous proteins whose functions have not yet been defined give important insight into elucidating the biochemical function of a new protein family which has highly conserved regions containing cysteine.
Lim
Y S
YS
Department of Biochemistry, Pai-Chai University, Taejon, South Korea.
Cha
M K
MK
Kim
H K
HK
Kim
I H
IH
D000595:Amino Acid Sequence; D000818:Animals; D000975:Antioxidants; D001483:Base Sequence; D001921:Brain / Q000378:metabolism*; D003001:Cloning, Molecular; D017124:Conserved Sequence; D003545:Cysteine / Q000032:analysis*; D004247:DNA; D004926:Escherichia coli; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010544:Peroxidases; D054464:Peroxiredoxins; D017386:Sequence Homology, Amino Acid
D000975:Antioxidants; D005656:Fungal Proteins; D004247:DNA; D010544:Peroxidases; D054464:Peroxiredoxins; D003545:Cysteine