FEBS Letters | |
2',3'‐Dialdehyde of GTP blocks regulatory functions of adenylate cyclase Ns protein | |
Bulargina, Tamara V.1  Skurat, Alexander V.1  Yurkova, Maria S.1  Severin, Eugene S.1  Khropov, Yuri V.1  | |
[1] Department of Biochemistry, Moscow State University, Moscow 119899, USSR | |
关键词: GTP 2'; 3'-dialdehyde; Adenylate cyclase; Ns; protein; Caudate nucleus; Forskolin; Reconstitution; | |
DOI : 10.1016/0014-5793(85)80893-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Preincubation of bovine caudate nucleus membranes with the 2',3'-dialdehyde of GTP (oGTP) reduces adenylate cyclase activation by guanylyl imidodiphosphate (GppNHp) in a time-dependent fashion. A slower rate of inhibition is observed if membranes are treated with both GTP and oGTP. The efficacy of oGTP action is enhanced by raising the Mg2+ concentration. Reduction of adenylate cyclase sensitivity to GppNHp is followed by an irreversible decrease of enzyme stimulation by forskolin. Addition of a Lubrol soluble preparation from guinea pig lung membranes to oGTP-treated caudate nucleus membranes causes restoration of the adenylate cyclase sensitivity to GppNHp. These data suggest that oGTP blocks the GTP-binding site of the adenylate cyclase system localized on the Ns protein. Such modification leads to the elimination of the Ns-mediated regulation of the enzyme.
【 授权许可】
Unknown
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