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Molecular Cloning of Mouse Placental Lactogen cDNA
Laurie L. Jackson, Peter Colosi, Frank Talamantes and Daniel I. H. Linzer
Proceedings of the National Academy of Sciences of the United States of America
Vol. 83, No. 22 (Nov. 15, 1986), pp. 8496-8500
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/29081
Page Count: 5
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We have isolated a cDNA clone for the 23-kDa mouse placental lactogen II (mPL-II) from a phage λ gt11 expression library containing cDNA synthesized from BALB/c placental RNA. Translation in vitro of placental mRNA selected by hybridization to the mPL-II cDNA clones yields a 26-kDa polypeptide that is the size of the expected precursor protein and that is immunoprecipitated with anti-mPL-II antiserum. The mPL-II cDNA clones hybridize to a 1.0-kilobase placental-specific mRNA. This mRNA, found in the fetal portion of the placenta, appears as early as day 10 of gestation and increases to a maximal level by day 12. The mPL-II cDNA nucleotide sequence has been determined. This sequence contains an open reading frame encoding a polypeptide of 222 amino acids with the amino-terminal 31 amino acids forming the signal sequence for secretion. The predicted secreted protein has 51% amino acid homology with mouse prolactin.
Proceedings of the National Academy of Sciences of the United States of America © 1986 National Academy of Sciences