A PAF‐acetylhydrolase activity in Tetrahymena pyriformis cells

FEBS Letters

Tsoukatos, Demokritos¹  Tselepis, Alexandros D.¹  Lekka, Marilena E.¹ 

[1] Laboratory of Biochemistry, Department of Chemistry, University of Ioannina, Ioannina 45110, Greece

关键词: Platelet-activating factor;    PAF;    Phospholipase A2;    PAF-acetylhydrolase;    Lipid metabolism;    (Tetrahymena pyriformis);    PAF;    platelet-activating factor;    PAF-AH;    PAF-acetylhydrolase;    PLA2;    phospholipase A2;    [3H]PAF;    1-O-hexadecyl-2-[3H]acetyl-sn-glycero-3-phosphocholine;    [3H]alkyl-PAF;    1-O-[1′;    2′-3H]hexadecyl-2-acetyl-sn-glycero-3-phosphocholine;    BSA;    bovine serum albumin;    TCA;    trichloroacetic acid;    DFP;    diisopropyl-fluorophosphate;    PMSF;    phenylmethylsulfonylfluoride;   

DOI  :  10.1016/0014-5793(91)81022-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Our study provides evidence for the existence of an acylhydrolase activity in Tetrahymena pyriformis cells, capable of hydrolizing the sn-2 ester bond of the PAF molecule. This activity is mainly distributed in the microsomal fraction (76.5% of total) and has properties similar to the mammalian PAF-acetylhydrolase since it is Ca²⁺-independent, acid-labile, is inhibited by DFP and PMSF but it is not affected by egg yolk phosphatidylcholine. This microsomal acylhydrolase has apparent K_m and V_max values of 1.56 μM and 373 pmols - mg - min respectively. This is the first report of the existence of a PAF-acetylhydrolase activity in a non-mammalian cell.

【 授权许可】

Unknown