CLONING AND EXPRESSION OF A CDNA CODING FOR A RAT-LIVER PLASMA-MEMBRANE ECTO-ATPASE - THE PRIMARY STRUCTURE OF THE ECTO-ATPASE IS SIMILAR TO THAT OF THE HUMAN BILIARY GLYCOPROTEIN-I

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  • 25 August 1989
    • journal article
    • research article
    • Vol. 264  (24) , 14408-14414
Abstract
The amino acid sequence of the ecto-ATPase from rat liver was deduced from analysis of cDNA clones and a genomic clone. Immunoblots with antibodies raised against a peptide sequence deduced from the cDNA sequence indicated that the determined amino acid sequence is that of the ecto-ATPase. The deduced sequence predicts a 519-amino acid protein with a calculated molecular mass of 57,388 daltons. There are 16 potential asparagine-linked glycosylation sites in the protein. Hydropathy analysis of the deduced amino acid sequence indicates that the protein has two hydrophobic stretches. One is located at the N-terminal and the other is near the C-terminal end. A full-length clone encoding the ecto-ATPase was expressed transiently in mouse L cells and human HeLa cells. The cell lysate from the transfected cells contained immunoreactive ecto-ATPase and Ca2+-stimulated ATPase activities. The expressed protein is glycosylated and has an apparent molecular weight (100,000) similar to that of the rat liver plasma membrane ecto-ATPase.

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