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    J Biochem. 1990 Aug;108(2):145-8.

    Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences.

    Takahashi K, Akasaka M, Yamamoto Y, Kobayashi C, Mizoguchi J, Koyama J.

    Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University.

    Human plasma glutathione peroxidase (GSHPx) has been shown to be a selenium-containing enzyme immunologically distinct from cellular GSHPx. Oligonucleotide probes, based on the partial amino acid sequence of plasma GSHPx, were synthesized and used to screen a human placenta cDNA library. Nucleotide sequence analysis of the obtained clones revealed that GSHPx consisted of a 678-base pair open reading frame coding for a 226-amino acid polypeptide with a Mr of 25,389. About 50% of the deduced amino acid sequence was confirmed by partial amino acid sequencing of the peptides in a lysine endopeptidase-digest of the purified enzyme. The amino acid sequence exhibited only 44% homology with that of human cellular GSHPx. Northern blot analysis revealed a single transcript of 2.2 kilobases in the poly(A)+ RNA fractions of human placenta and HepG2 (a human hepatic cell line), but not that of human liver and endothelial cells.

    PMID: 2229017 [PubMed - indexed for MEDLINE]

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