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We have isolated a novel cDNA from human myeloma cells encoding a member of the reprolysin family of metalloproteinases. Derived amino acid sequence predicts a protein of approx. 76 kDa. The open reading frame predicts the presence of a leader peptide, a pro-peptide with a 'cysteine switch', a metalloproteinase domain, a disintegrin-like domain, a cysteine-rich domain, an epidermal growth factor-like domain and a putative transmembrane sequence. Expression of the mRNA for this metalloproteinase has been demonstrated in human myeloma cells.

Original publication

DOI

10.1042/bj3180459

Type

Journal article

Journal

Biochem j

Publication Date

01/09/1996

Volume

318 ( Pt 2)

Pages

459 - 462

Keywords

Amino Acid Sequence, Base Sequence, Blotting, Northern, Cell Line, Cell Membrane, Cloning, Molecular, DNA Primers, Disintegrins, Female, Gene Library, Humans, Metalloendopeptidases, Molecular Sequence Data, Multiple Myeloma, Placenta, Polymerase Chain Reaction, Pregnancy, Recombinant Proteins, Sequence Homology, Amino Acid, Tumor Cells, Cultured