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    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/26368


    Title: Biochemical properties and expression profile of human prolyl dipeptidase DPP9
    Authors: Tang,HK;Tang,HY;Hsu,SC;Chu,YR;Chien,CH;Shu,CH;Chen,X
    Contributors: 化學工程與材料工程學系
    Keywords: PEPTIDASE-IV;MOLECULAR CHARACTERIZATION;PURIFICATION;INHIBITION;IDENTIFICATION;LOCALIZATION;ISOINDOLINE;SPECIFICITY;SELECTIVITY;PROTEINS
    Date: 2009
    Issue Date: 2010-06-29 17:26:30 (UTC+8)
    Publisher: 中央大學
    Abstract: Dipetidyl peptidase 9 (DPP9) is a prolyl dipeptidase preferentially cleaving the peptide bond after the penultimate proline residue. The biological function of DPP9 is unknown. In this study, we have significantly improved the yield using Strep-Tactin (R) purification system and characterized the biochemical property of DPP9. Moreover, the dimer interaction mode was investigated by introducing a mutation (F842A) at the dimer interface, which abolished the enzymatic activity without disrupting its quaternary structure. Furthermore, DPP9 was found ubiquitously expressed in fibroblasts, epithelial, and blood cells. Surprisingly, contrary to previous report, we found that the expression levels of DPP8 and DPP9 did not change upon the activation of the PBMC or Jurkat cells. These results indicate that the biochemical property of DPP9 is very similar to that of DPP8, its homologous protease. DPP9 and DPP8 are likely redundant proteins carrying out overlapping functions in vivo. (C) 2009 Elsevier Inc. All rights reserved.
    Relation: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
    Appears in Collections:[化學工程與材料工程研究所] 期刊論文

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