國家衛生研究院 NHRI:Item 3990099045/3555
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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/3555


    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: Division of Biotechnology and Pharmaceutical Research;Vaccine Research and Development Center
    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·TactinR 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.
    Date: 2009-05-15
    Relation: Archives of Biochemistry and Biophysics. 2009 May 15;485(2):120-127.
    Link to: http://dx.doi.org/10.1016/j.abb.2009.02.015
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0003-9861&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000265949100005
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=65649088506
    Appears in Collections:[Xin Chen(2002-2015)] Periodical Articles
    [Shu-Ching Hsu] Periodical Articles

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