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Fakulteta za farmacijo, Ljubljana (FFALJ)
  • Cloning and expression of functional equistatin
    Galeša, Katja ...
    Equistatin is a 1999-residue protein composed of three thyroglobulin type-1 domains. It strongly inhibits cysteine proteinases as well as the aspartic proteinase cathepsin D. In order to initiate ... structure-function studies by protein engineering, a cDNA library from sea anemone, Actinia equina, was screened. A positive clone of 888 nucleotides was shown to encode a protein of 231 amino acids, including the signal sequence. The mature protein region was amplified by PCR, cloned into the pET22b(+)cas expression vector and expresses in Escherichia coli. Isolation of active recombinant equistatin required only one purification step, the His-tag affinity column. The protein displays physical and inhibitory properties closely similr to the native inhibitor.
    Vir: Biological chemistry. - ISSN 1431-6730 (Vol. 381, no. 1, 2000, str. 85-88)
    Vrsta gradiva - članek, sestavni del ; neleposlovje za odrasle
    Leto - 2000
    Jezik - angleški
    COBISS.SI-ID - 617841

vir: Biological chemistry. - ISSN 1431-6730 (Vol. 381, no. 1, 2000, str. 85-88)

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