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    Biochem J. 1991 Aug 1;277 ( Pt 3):631-4.

    Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide.

    Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ.

    Source

    Department of Histopathology, St. George's Hospital Medical School, London, U.K.

    Abstract

    Tartrate-resistant acid phosphatases have been isolated from a number of sources. These enzymes consist of one subunit (Mr 30,000-40,000) or two dissimilar subunits (Mr 15,000-20,000). Previously we isolated the enzyme from human osteoclastomas, as a two-subunit protein. By Northern blotting and hybridization with radiolabelled oligonucleotides corresponding to the N-terminal sequences of the two subunits, we demonstrate here that the enzyme is transcribed as one mRNA which is translated in vitro to produce a single polypeptide of approx. Mr 33,000. Transcription as a single mRNA species is also the case in other tissues. These results suggest that the osteoclastoma enzyme undergoes post-translational modification in the form of cleavage of a single peptide bond to give a disulphide-bonded two-subunit protein.

    PMID:
    1872798
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC1151288
    Free PMC Article

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