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- W1768761279 abstract "Two high-affinity cAMP-binding proteins (I and II) have been purified to homogeneity from baker's yeast by a procedure avoiding proteolytic damage. These proteins have been identified as multiple forms of glyceraldehyde-3-phosphate dehydrogenase. The two cAMP-binding proteins are similar in affinities for cAMP, have identical elution volumes on gel filtration, and contain one type of subunit (Mr 37 500). The form II of glyceraldehyde-3-phosphate dehydrogenase is free of NAD+ and has a Kd of 1.3 X 10(-6) M with respect to cAMP. A marked concentration-dependent self-association of the subunits of the form-II protein was revealed by Yphantis sedimentation equilibrium studies. Significant monomer concentrations are present at total concentrations less than 0.02 mg/ml. Conventional sedimentation equilibrium analyses indicated a tetramer Mr of 170 000. The high-affinity binding of cAMP to glyceraldehyde-3-phosphate dehydrogenase may significantly reduce intracellular cAMP levels and is also discussed in relation to the nature of eukaryote cAMP-binding proteins with similar native or subunit Mr values which are at present functionally undefined." @default.
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- W1768761279 date "1980-08-01" @default.
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- W1768761279 title "Purification and Characterization of Two High-Affinity (Adenosine 3',5'-Monophosphate)-Binding Proteins from Yeast. Identification as Multiple Forms of Glyceraldehyde-3-Phosphate Dehydrogenase" @default.
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- W1768761279 doi "https://doi.org/10.1111/j.1432-1033.1980.tb04765.x" @default.
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