Molecular cloning of cDNA coding for rat plasma glutathione peroxidase.
The plasma glutathione peroxidase (PGSH-PO), which is different from erythrocyte glutathione peroxidase (EGSH-PO) in immunochemical property and substrate specificity, was purified from male Wistar rat serum. The amino acid sequence of 5 independent peptides were determined and a cDNA clone for this enzyme was isolated from placental cDNA library. The nucleotide sequence of the cDNA revealed that, similar to EGSH-PO cDNA, the seleno-cysteine was genetically encoded by "TGA" codon. On comparing the nucleotide sequences of EGSH-PO and PGSH-PO, no significant homology was found in the vicinities of "TGA" codons of both enzymes.
Yoshimura
S
S
Department of Cell Biology, Tokai University School of Medicine, Kanagawa, Japan.
Onozawa
T
T
Mizoguchi
J
J
Suemizu
H
H
Moriuchi
T
T
Watanabe
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon; D004247:DNA; D005979:Glutathione Peroxidase / Q000097:blood / Q000235:genetics*; D008297:Male; D008969:Molecular Sequence Data; D051381:Rats; D011919:Rats, Inbred Strains; D012689:Sequence Homology, Nucleic Acid
D003062:Codon; D004247:DNA; D005979:Glutathione Peroxidase