Chemical Research in Chinese Universities ›› 2005, Vol. 21 ›› Issue (3): 291-293.

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Research on the Role of Rat TPP-Ⅰ in Neuromedin B Degradation

DU Pei-ge1, QIU Fang-ping2, AN Li-ping1, WANG Yan1, LU Gang1   

  1. 1. Pharmaceutical College of Beihua University, Jilin 132000, P. R. China;
    2. College of Biological Engineering, Changchun University of Technology, Changchun 130012, P. R. China
  • Received:2004-08-02 Online:2005-05-24 Published:2011-08-06
  • Supported by:

    Supported by the Scientific Research Fund for the Returned Overseas Chinese Scholars, State Education Ministry.

Abstract: TPP-Ⅰ(tripeptidyl peptidase-Ⅰ) protein turnover was studied by observing the role of rat TPP-Ⅰ in neuromedin B(NMB) and other neuropeptides degradations in some physiological situations. The mixtures of rat TPP-Ⅰ with each of NMB, other neuropeptides and Ala-Ala-Phe-MCA were made respectively under the same conditions. The reaction was observed at different timeand monitored by means of high performance liquid chromatography(HPLC) and time-of-flight mass spectrometry(TOF-MS) in vitro. NMB was broken down at the same degree as Ala-Ala-Phe-MCA by rat TPP-Ⅰ and Gly-Asn-Leu was released within 16 h, but other neuropeptides were not digested within 24 h. TPP-Ⅰ is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B. NMB has recently been found to be a good natural substrate for rat lysosomal TPP-Ⅰ.

Key words: Rat, Tripeptidyl peptidase-Ⅰ, Neuromedin B, Late-infantile neuronal ceroid lipofuscinosis, Degradation