FEBS Letters | |
Interaction of GTP‐binding proteins with calmodulin | |
Ogasawara, Nobuaki1  Kitajima, Satoko2  Sano, Mamoru2  Asano, Tomiko1  | |
[1] Department of Biochemistry, Institute for Developmental Research, Aichi Prefectural Colony, Kasugai, Aichi 480-03, Japan;Department of Morphology, Institute for Developmental Research, Aichi Prefectural Colony, Kasugai, Aichi 480-03, Japan | |
关键词: GTP-binding protein; Calmodulin; Cyclic nucleotide phosphodiesterase; Protein interaction; | |
DOI : 10.1016/0014-5793(86)80729-3 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Two GTP-binding proteins (Gi and Go), which were the substrates for islet-activating protein, pertussis toxin, were purified from bovine cerebral cortical membranes. Both Gi and Go completely inhibited calmodulin-stimulated cyclic nucleotide phosphodiesterase activity. The same concentrations of these proteins, however, had no appreciable effect on the basal phosphodiesterase activity. The isolated Giα and βγ subunits of GTP-binding proteins were potent inhibitors of the calmodulin-stimulated phosphodiesterase activity, but Goα was very weak. Therefore, the βγ subunits were likely to be the major active molecules in the brain membranes. GTP-binding proteins were shown to bind directly to calmodulin in a Ca2+-dependent manner by a gel permeation binding experiment.
【 授权许可】
Unknown
【 预 览 】
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RO201912020288219ZK.pdf | 360KB | download |