An adenosine 3':5'-monophosphate-adenosine binding protein from mouse liver.
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چکیده
منابع مشابه
An adenosine 3':5'-monophosphate adenosine-binding protein from mouse liver. Association with S-adenosylhomocysteinase activity.
Cyclic AMP-binding proteins not associated with protein kinase activity have been described in various tissues [l-7 1. Most of these proteins have been shown to bind adenosine [3,6,7]. We have purified to apparent homogeneity a cyclic AMP adenosine-binding protein from mouse liver 273. The molecular properties of this protein and its interaction with adenosine, adenine and adenine nucleotides h...
متن کاملAn adenosine 3':5'-monophosphate-adenosine binding protein from mouse liver: some physicochemical properties.
A number of physiochemical properties of the cyclic AMP-adenosine binding protein of mouse liver (Ueland, P.M. and Døskeland, S.O. (1977) J. Biol. Chem. 252, 677--686) have been studied. 1. The specific extinction coefficient, E1%280nm, was estimated to 13.0. 2. Amino acid and amide group analyses confirmed the acidic properties of the protein as determined by electrofocusing (pI = 5.7). Based ...
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A simple and sensitive assay for adenosine 3':5'-cyclic monophosphate (cAMP) has been developed that is based on competition for protein binding of the nucleotide, presumably to a cAMP-dependent protein kinase. The nucleotide-protein complex is adsorbed on a cellulose ester filter. Assay conditions are such that a binding constant approaching 10(-9) M is obtained, and the assay is thus sensitiv...
متن کاملDifferential binding of cyclic adenosine 3' ,5'-monophosphate to the cyclic adenosine 3' ,5'-monophosphate receptor protein in Escherichia coli.
Binding of cyclic adenosine 3' ,5'-monophosphate (cAMP) by the cAMP receptor protein in crude cell-free extracts of Escherichia coli was characterized. When cell were grown in glucose, binding was inhibited 50% relative to extracts from cells grown with succinate as carbon source . This inhibition could be relieved by dialysis.
متن کاملRegulation of cyclic adenosine 3':5'-monophosphate-binding protein in N-18 mouse neuroblastoma cells.
The regulation of cyclic adenosine 3':5'-monophosphate (cAMP)-binding protein in N-18 neuroblastoma cells in tissue culture was studied by the covalent incorporation of 8-azido-cyclic adenosine 3':5'-[32P]monophosphate, together with the techniques of sodium dodecyl sulfate:polyacrylamide gel electrophoresis and autoradiography. Greater than 95% of the total cAMP binding activity of N-18 neurob...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)32772-2