pH dependence of bovine mast cell tryptase catalytic activity and of its inhibition by 4′,6‐diamidino‐2‐phenylindole

FEBS Letters

Erba, Fulvio²  Bolognesi, Martino¹  Fiorucci, Laura²  Ascoli, Franca² 

[1] Advanced Biotechnology Centre and Department of Physics, University of Genova, viale Benedetto XV 10, I-16132, Genova, Italy;Department of Experimental Medicine and Biochemical Sciences, University ‘Tor Vergata’, via di Tor Vergata 135, I-00133, Rome, Italy

关键词: Bovine tryptase;    4′;    6-Diamidino-2-phenylindole;    Catalytic activity;    Inhibitor;    DAPI;    4′;    6-diamidino-2-phenylindole;    BABIM;    bis-(5-amidino-2-benzimidazolyl)-methane;    DAPP;    1;    3-bis(p-amidinophenoxy)-propane;    Boc-Phe-Ser-Arg-MCA;    t-butyloxy-carbonyl-Phe-Ser-Arg-7-amido-4-methyl-coumarin;    MCA;    7-amino-4-methyl-coumarin;   

DOI  :  10.1016/S0014-5793(97)00395-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tryptases are oligomeric enzymes localized in the secretory granules of mast cells. Their role(s) in vivo has yet to be clarified and the lack of powerful and specific inhibitors has hampered the comprehension of the biological functions of these enzymes. In this paper, we identify 4′,6-diamidino-2-phenylindole as a potent inhibitor for bovine tryptase. This inhibitory effect and the enzyme catalyzed hydrolysis of the synthetic substrate Boc-Phe-Ser-Arg-methyl-coumarin were investigated in the pH range of 6.0–9.0. On the basis of the pK shifts occurring upon formation of the inhibitor(substrate)/enzyme complexes, some aminoacidic groups are proposed to play a role in such interactions.

【 授权许可】

Unknown