J. Biochem, 1990, Vol. 108, No. 2 145-148
© 1990 Japanese Biochemical Society
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Primary Structure of Human Plasma Glutathione Peroxidase Deduced from eDNA Sequences1
*Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University Kita-ku, Sapporo, Hokkaido 060
**Research Laboratory, Toyo Jozo Co., Ltd. Ohito, Shizuoka 410-23
Human plasma glutathione peroxidase (GSHPx) has been shown to be a selenium-containing enzyme immunologically distinct from cellular GSIIPx. 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 th 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.
1This work was in part supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.
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