Evidence for complex formation between GTP binding protein(Gs) and membrane-associated nucleoside diphosphate kinase.
Evidence for complex formation between GTP binding protein(Gs) and membrane-associated nucleoside diphosphate kinase.
复制标题
GTP 结合蛋白 (Gs) 和膜相关核苷二磷酸激酶之间形成复合物的证据。
DOI:
10.1016/0006-291x(90)91680-q
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发表时间:
1990
影响因子:
3.1
通讯作者:
N. Shimada
中科院分区:
文献类型:
--
作者:
Narimichi Kimura;N. Shimada
When the Gs in rat liver membranes was prelabeled with [32P]NAD and cholera toxin, solubilized with octylglucoside, and then analyzed by sucrose density gradient centrifugation, it was fractionated into two peaks with approximate molecular sizes of 12–13S and 3–4S. Pretreatment without or with GDPβS of the labeled membranes resulted in a larger peak in the high molecular weight region, whereas pretreatment with glucagon plus GTPτS caused almost equal peaks in both regions. The affinity-purified anti-nucleoside diphosphate(NDP) kinase antibodies only precipitated the Gs in high molecular weight region. Under the same condition, small but significant NDP kinase activity was associated with the high molecular weight Gs region although a large portion of the enzyme activity was recovered in fractions where it alone should appear(6.2S). Both Lubrol-PX and digitonin solubilized the Gs in forms insensitive to immunoprecipitation by anti-NDP kinase antibodies although the latter detergent was able to solubilize the Gs in a high molecular weight form, that is, a ternary glucagon-receptor-G protein complex. These results demonstrate that Gs and membrane-associated NDP kinase may exist in part in a complexed form in membranes. Physiological relevance of the complex formation in membrane signal transduction is discussed.
DOI:
--
发表时间:
1984
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Bokoch,GM;Katada,T;Northup,JK;Ui,M;Gilman,AG
通讯作者:
Gilman,AG