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在血管肌肉微粒体组分中,质膜成分是四氧嘧啶作用于ATP驱动的Ca2+转运的主要作用位点。

The plasma-membrane component is the primary site of action of alloxan on ATP-driven Ca2+ transport in vascular-muscle microsomal fractions.

作者信息

Kwan C Y

机构信息

Department of Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.

出版信息

Biochem J. 1988 Aug 15;254(1):293-6. doi: 10.1042/bj2540293.

Abstract

The direct effects of alloxan in vitro on the handling of Ca2+ by microsomal fractions from dog aortic smooth muscle were investigated. Preincubation of the vascular-muscle microsomal membranes with alloxan showed a suppression of both binding of Ca2+ (in the absence of ATP) and ATP-driven Ca2+ transport. Alloxan substantially inhibited the microsomal ATP-driven Ca2+ transport stimulated by Pi, but not that stimulated by oxalate. Studies using subfractions isolated from the microsomal membranes on a sucrose density gradient indicated that plasma membrane is the primary site of action of alloxan on the ATP-driven Ca2+ transport.

摘要

研究了四氧嘧啶在体外对犬主动脉平滑肌微粒体组分处理Ca2+的直接影响。用四氧嘧啶对血管肌肉微粒体膜进行预孵育,结果显示Ca2+结合(在无ATP的情况下)和ATP驱动的Ca2+转运均受到抑制。四氧嘧啶显著抑制了由Pi刺激的微粒体ATP驱动的Ca2+转运,但对草酸盐刺激的Ca2+转运没有抑制作用。利用在蔗糖密度梯度上从微粒体膜分离的亚组分进行的研究表明,质膜是四氧嘧啶对ATP驱动的Ca2+转运作用的主要位点。

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Am J Physiol. 1980 Sep;239(3):C66-74. doi: 10.1152/ajpcell.1980.239.3.C66.
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