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    Biochim Biophys Acta. 1992 Sep 24;1132(2):154-60.

    Sequence and expression of human protein kinase C-epsilon.

    Basta P, Strickland MB, Holmes W, Loomis CR, Ballas LM, Burns DJ.

    Source

    Sphinx Pharmaceuticals Corporation, Molecular Biology Section, Durham, NC 27717.

    Abstract

    Two human homologues of protein kinase C-epsilon (E1 and E2) were isolated from two distinct cDNA libraries. Sequence comparisons to PKC-epsilon cDNAs from several species indicated that each of these human epsilon clones contained cloning artifacts. Thus, a composite PKC-epsilon (E3) clone was derived from clones E1 and E2. Human PKC-epsilon (E3) has an overall sequence identity of 90-92% at the nucleotide level compared to the previously characterized mouse, rat and rabbit clones. At the amino acid level, the deduced human epsilon sequence shows a 98-99% identity with the mouse, rat and rabbit sequences. Expression of the human PKC-epsilon clone in Sf9 cells confirmed that the recombinant protein displayed protein kinase C activity and phorbol ester binding activity. The recombinant protein was also recognized by two distinct epsilon-specific polyclonal antibodies.

    PMID:
    1382605
    [PubMed - indexed for MEDLINE]

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