國家衛生研究院 NHRI:Item 3990099045/3396
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    题名: Purification and characterization of a dipeptidyl peptidase 9-like enzyme from bovine testes
    作者: Dubois, V;Lambeir, AM;Van Der Veken, P;Augustyns, K;Creemers, J;Chen, X;Scharp, S;De Meester, I
    贡献者: Division of Biotechnology and Pharmaceutical Research
    摘要: Until now, only recombinant forms of dipeptidyl peptidase (DPP) 8 and 9 have been characterized. We purified non DPPII-non DPPIV enzymes from a natural source. A first DPP8/9-like enzyme was enriched 1160-fold from bovine testes and identified as 'DPP9-like enzyme' by using an anti-DPP9 antibody. A second 576-fold enriched preparation ('DPP enriched peak 3') also showed DPP8/9-like activity. SDS-PAGE analysis showed that the DPP9-like enzyme had a monomelic molecular mass of approx. 100 kDa. Size exclusion chromatography generated a native molecular mass of 164 kDa for the DPP9-like enzyme and one of 234 kDa for the DPP enriched peak 3, suggesting that both proteins appeared to be dimeric. Both enriched preparations and rDPP8 showed roughly similar substrate specificity and inhibitor profiles. The DPP9-like enzyme and the DPP enriched peak 3 possessed a neutral pH optimum and were stable at -80?C We can conclude that the natural DPP9-like enzyme and the DPP enriched peak 3 are closely related to the recombinant forms of human DPP9 and DPP8.
    日期: 2008-05-01
    關聯: Frontiers in Bioscience. 2008 May 1;13(9):3558-3568.
    Link to: http://dx.doi.org/10.2741/2949
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=2768-6701&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000255885000030
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=42649117199
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