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The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions
Authors:Yoo-Shick Lim   Mee-Kyung Cha   Ha-Kun Kim  Il-Han Kim  
Affiliation:

a Departments of Biochemistry, Pai-Chai University, Taejon 302-735, South Korea

b Genetic Engineering, Pai-Chai University, Taejon 302-735, South Korea

Abstract:The complete cDNA encoding human thiol-specific antioxidant protein (PRP) was isolated from a human brain cDNA library in the λZap expression vector. An open reading frame (ORF) was identified and found to encode a polypeptide of 197 aa with a Mr 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.
Keywords:cDNA   sequencing   functional expression   homologous protein   activated oxygen species
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