Mouse placental lactogen-I (mPL-I) cDNA was inserted into a eukaryotic expression vector and introduced into Chinese hamster ovary cells. Cell lines that secrete high concentrations of mPL-I were isolated, and this glycoprotein was purified from the cell culture-conditioned medium. Recombinant mPL-I (mPL-Ir) is very similar to placental mPL-I (mPL-IP) in its recognition by polyclonal antisera raised against either mPLP Ip or mPL-Ir, in displacing [125I]iodo-mPL-II from binding sites on mouse liver microsomal membranes, and in stimulating the synthesis of α-lactalbumin in primary cultures of mouse mammary epithelial cells. Structural comparison of mPL-Ir and mPL-IP by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that mPL-Ir comprises several proteins with mol wt ranging from 34.5-38K, while mPL-IP consists of a similar set of proteins with mol wt ranging from 36.5-42K. Treatment of the two proteins with neuraminidase resulted in similar 2-4K decreases in mol wt. Treatment of mPL-IP with peptide:N-glycosidase-F to remove asparagine-linked oligosaccharide chains resulted in the formation of 28K and 29K mol wt species, while treatment of mPL-Ir with the same enzyme yielded 28K and 28.5K mol wt products.
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