| Literature DB >> 8144038 |
Y S Lim1, M K Cha, H K Kim, I H Kim.
Abstract
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.Entities:
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Year: 1994 PMID： 8144038 DOI： 10.1016/0378-1119(94)90558-4
Source DB: PubMed Journal: Gene ISSN： 0378-1119 Impact factor: 3.688