Activation of turkey erythrocyte adenylate cyclase and blocking of the catecholamine-stimulated GTPase by guanosine 5'-(gamma-thio) triphosphate. |
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| Authors: | D Cassel Z Selinger |
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| Affiliation: | Institute of Biochemistry, Faculty of Medicine, University of Nagoya, Nagoya 466, Japan |
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| Abstract: | By SDS-polyacrylamide gel electrophoresis, mitochondrial proteins having covalently-bound flavin were analyzed. Mitochondria were prepared from the liver of rat injected with radioactive riboflavin. Radioactivity was found to be associated with four protein components. Their subunit molecular weights were 91,000, 72,000, 60,000 and 44,000. The first two components exhibited yellowish fluorescence on a gel under ultraviolet illumination. The component of the highest molecular weight seems to be a new protein containing covalently-bound flavin. |
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| Keywords: | App(NH)p and Gpp(NH)p adenosine and guanosine 5′-(β, γ-imino) triphosphate respectively GTPγS guanosine 5′-(γ-thio) triphosphate NTPase nucleoside triphosphatase |
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