Purification of a heat‐stable activator protein for ADP‐ribosylation factor‐dependent phospholipase D

FEBS Letters

Nakamura, Shun-ichi¹  Hitomi, Tomohiro¹  Miwa, Noriko¹  Yoshida, Kimihisa¹  Jinnai, Hitoshi¹  Akisue, Toshihiro¹ 

[1] Department of Biochemistry, Kobe University School of Medicine, Kobe 650, Japan

关键词: Phospholipase D;    ADP-ribosylation factor;    Phospholipase D activator;    Phosphatidylcholine;    Phosphatidylethanolamine;    PtdCho;    phosphatidylcholine;    PLD;    phospholipase D;    ARF;    ADP-ribosylation factor;    PtdIns-4;    5-P2;    phosphatidylinositol 4;    5-bisphosphate;    PtdEtn;    phosphatidylethanolamine;    G-protein;    GTP-binding regulatory protein;    PKC;    protein kinase C;    GTP-γ-S;    guanosine 5′-O-(3-thiotriphosphate);    [14C]PtdCho;    1;    2-di-[1-14C]palmitoyl-sn-glycero-3-phosphocholine;    [14C]lysoPtdCho;    1-[1-14C]palmitoyl-2-lyso-sn-glycero-3-phosphocholine;    PtdEtOH;    phosphatidylethanol;    PMA;    phorbol 12-myristate 13-acetate;    Octylglucoside;    1-octyl β-glucopyranoside;   

DOI  :  10.1016/S0014-5793(97)01611-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A heat-stable activator for ADP-ribosylation factor (ARF)-dependent phospholipase D (PLD) was purified to near homogeneity from rat kidney cytosol by a sequential column chromatography. The purified activator has a molecular mass of 23 kDa on SDS-PAGE. Using a partially purified ARF-dependent PLD from rat kidney, the activator synergistically stimulates PLD with ARF in time- and dose-dependent manner. In the absence of ARF, the activator has little or no effect. The purified activator also stimulates PLD under several conditions including permeabilized cell system, suggesting that the activator is a physiologically relevant regulator of PLD.

【 授权许可】

Unknown