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 (P RP) was isolated from a human brain cDNA library in the lambdaZap expr ession 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 contai ned 98 bp of 5'-untranslated sequence (UTR) and 259 bp of 3'-UTR conta ining a poly(A) signal, AATAAA. Expression of the human PRP cDNA in Es cherichia coli yielded a functionally active protein. The observed loc al 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 ha s highly conserved regions containing cysteine.