Involvement of GTP-regulatory protein in brain prostaglandin E2 receptor and separation of the two components |
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| Authors: | N Yumoto M Hatanaka Y Watanabe O Hayaishi |
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| Institution: | 1. Department of Medical Biotechnology, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran;2. Pharmaceutical Research Center and School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran;3. Biotechnology Research Center, Mashhad University of Medical Sciences, Mashhad, Iran;1. Department of Earth Resources Engineering, Kyushu University, Fukuoka 819-0395, Japan;2. Department of Geological Engineering, Universitas Gadjah Mada, Yogyakarta 55281, Indonesia;3. PT Geo Dipa Energi (Persero), Jakarta 12510, Indonesia;4. Department of Chemistry, Kyushu University, Faculty of Science, Fukuoka 819-0395, Japan |
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| Abstract: | The specific binding protein for prostaglandin (PG) E2 solubilized from porcine brain was sensitive to guanine nucleotides. GTP inhibited the association and enhanced the dissociation of the specific 3H]PGE2 binding. Scatchard analyses showed that GTP (10 microM) decreased the binding affinity more than 3-fold without major change in the number of binding site. Gel filtration separated the binding site from GTP-regulatory component (N). The separated binding protein had a reduced affinity to PGE2 and lost its sensitivity to GTP. The addition of the separated N restored its responsiveness to GTP, and also increased the binding affinity to the original level. These results provide direct evidence for the molecular interaction between the PGE2 binding protein and N in the brain. |
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