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• W1970709570 abstract "Both a fluorescence-quenching technique and a uv-difference spectral method have been used to study the binding of 1,N6-etheno analogs of the adenine nucleotides (ϵATP, ϵADP, ϵAMP) (J. A. Secrist III, J. R. Barrio, N. J., Leonard, and G. Weber, 1972, Biochemistry, 11, 3499–3506) to crystalline rabbit and calf muscle ATP-AMP transphosphorylase in the presence and absence of Mg2+, at 0.16 (Γ2), 25 °C, and pH 7.4. In addition, the binding of the ϵ-analogs of the adenine nucleotides has been studied to two S-[14C]carboxymethylated peptide fragments of the rabbit muscle enzyme (residues 1–44 = MT-I; residues 171–193 = MT-XII), as well as to a synthetic nonapeptide corresponding to residues 32 − 40 of the rabbit muscle enzyme. In the case of the rabbit and calf enzymes: MgϵATP2−, ϵATP4−, MgϵADP−, and ϵAMP2− are bound stoichiometrically (n ∼- 1), MgϵAMP is insignificantly bound, and n ∼- 2 for ϵADP3− (n = maximal number of moles bound per mole of protein). In the case of S-carboxymethylated peptide fragments: MT-I binds stoichiometrically to MgϵATP2−, ϵATP4−, MgϵADP−, and ϵADP3− with values of n ∼- 1; but MT-I does not bind to ϵAMP2− significantly. MT-XII binds stoichiometrically to uncomplexed ϵAMP2− or to uncomplexed ϵADP3− (both with n ∼- 1); whereas, the binding of MgϵADP−, ϵATP4−, and MgϵAMP to MT-XII are comparatively insignificant. Other peptide fragments in the molecule, viz. fragments MT-IV (residues 77–96) or MT-VI (residues 106–126) did not bind significantly to any of the ethenoanalogs; nor did insulin, nor, e.g., did bo vine serum albumin. The binding of the etheno analogs was also studied to an equimolar mixture of peptides MT-I + MT-XII, which qualitatively duplicated the binding pattern of the entire native molecule, and except for ϵATP4− or MgϵATP2− (which are bound more tightly to the entire native molecule), even quantitatively. The synthetic peptide (residues 32 to 40) was found to bind to MgϵATP2−, ϵATP4−, and MgϵADP−, with n ∼- 1; but it does not significantly bind to ϵAMP2−, nor to ϵADP3−. These binding data support the idea that there are two separate sites for the binding of either (a) the complexed nucleotide substrate (MgATP2− or MgADP−) residing in the sequence of MT-I (residues 1 to 44) and in the neighborhood of residues 32 to 40, or (b) the uncomplexed nucleotide substrate (AMP2− or ADP3−) residing in the sequence of MT-XII (residues 171 to 193) of the rabbit muscle enzyme." @default.
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• W1970709570 date "1979-06-01" @default.
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• W1970709570 title "Studies on adenosine triphosphate transphosphorylases XIV. Equilibrium binding properties of the crystalline rabbit and calf muscle ATP-AMP transphosphorylase (adenylate kinase) and derived peptide fragments" @default.
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• W1970709570 doi "https://doi.org/10.1016/0003-9861(79)90338-2" @default.
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