title: Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide.
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.
authors.affiliation: Department of Histopathology, St. George's Hospital Medical School, London, U.K.
authors.forename: A R
authors.initials: AR
authors.lastname: Hayman
authors.forename: A J
authors.initials: AJ
authors.lastname: Dryden
authors.forename: T J
authors.initials: TJ
authors.lastname: Chambers
authors.forename: M J
authors.initials: MJ
authors.lastname: Warburton
mesh_terms: D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics*; D001483:Base Sequence; D015152:Blotting, Northern; D005870:Giant Cell Tumors / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009841:Oligonucleotides / Q000737:chemistry; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000235:genetics; D012334:RNA, Neoplasm / Q000235:genetics; D013644:Tartrates / Q000494:pharmacology*
chemical_list: D009841:Oligonucleotides; D012333:RNA, Messenger; D012334:RNA, Neoplasm; D013644:Tartrates; D000135:Acid Phosphatase