A soluble ecto-ATPase from Tetrahymena thermophila: purification and similarity to the membrane-bound ecto-ATPase of smooth muscle.
A soluble ecto-ATPase from Tetrahymena thermophila: purification and similarity to the membrane-bound ecto-ATPase of smooth muscle.
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来自嗜热四膜虫的可溶性外源 ATP 酶:纯化及其与平滑肌膜结合外源 ATP 酶的相似性。
DOI:
10.1006/abbi.1996.9779
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发表时间:
1997
影响因子:
3.9
通讯作者:
Hennessey,TM
中科院分区:
文献类型:
--
作者:
SmithJr,TM;Kirley,TL;Hennessey,TM
Purinergic agonists, such as ATP, are considered to be fast trophoresis and approximately 69,000 Da by size ex-excitatory neurotransmitters in both the central and periph-clusion chromatography of the native form. The puri-eral nervous systems (2) and intercellular modulators of fied soluble enzyme displays the general characteris-many other cell functions. The general importance of pu-tics of a dedicated E-type ecto-ATPase such as Ca2/rinergic reception is seen in the involvement of nucleoside or Mg2/dependence, hydrolysis of ATP and other nu- triphosphates on cardiac, vascular and smooth muscle, excit-cleoside triphosphates (but not nucleoside diphos- atory and inhibitory effects on neurons, and effects on ion, phates) and insensitivity to common ATPase inhibi- hormone, exocrine gland, platelet, mast cell, and inflamma-tors (vanadate, azide, ouabain, N-ethylmaleimide and tory cell secretions (3). p-chloromercuriphenyl sulfonate). It was further Since Tetrahymena can detect and respond (in a chemore-shown to be immunologically similar (by polyclonal pellent assay) to nanomolar concentrations of GTP in their antibodies) to both the membrane-bound ecto- extracellular environment (4), we have been interested in