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
Archives of Biochemistry and Biophysics, ISSN: 0003-9861, Vol: 195, Issue: 1, Page: 155-177
1979
- 51Citations
- 5Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations51
- Citation Indexes51
- 51
- CrossRef47
- Captures5
- Readers5
Article Description
Both a fluorescence-quenching technique and a uv-difference spectral method have been used to study the binding of 1, N 6 -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 Mg 2+, 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 -[ 14 C]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: MgϵATP 2−, ϵATP 4−, MgϵADP −, and ϵAMP 2− are bound stoichiometrically ( n ∼- 1), MgϵAMP is insignificantly bound, and n ∼- 2 for ϵADP 3− ( n = maximal number of moles bound per mole of protein). In the case of S -carboxymethylated peptide fragments: MT-I binds stoichiometrically to MgϵATP 2−, ϵATP 4−, MgϵADP −, and ϵADP 3− with values of n ∼- 1; but MT-I does not bind to ϵAMP 2− significantly. MT-XII binds stoichiometrically to uncomplexed ϵAMP 2− or to uncomplexed ϵADP 3− (both with n ∼- 1); whereas, the binding of MgϵADP −, ϵATP 4−, 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 ϵATP 4− or MgϵATP 2− (which are bound more tightly to the entire native molecule), even quantitatively. The synthetic peptide (residues 32 to 40) was found to bind to MgϵATP 2−, ϵATP 4−, and MgϵADP −, with n ∼- 1; but it does not significantly bind to ϵAMP 2−, nor to ϵADP 3−. These binding data support the idea that there are two separate sites for the binding of either (a) the complexed nucleotide substrate (MgATP 2− 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 (AMP 2− or ADP 3− ) residing in the sequence of MT-XII (residues 171 to 193) of the rabbit muscle enzyme.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0003986179903382; http://dx.doi.org/10.1016/0003-9861(79)90338-2; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0018483548&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/224811; https://linkinghub.elsevier.com/retrieve/pii/0003986179903382; http://dx.doi.org/10.1016/0003-9861%2879%2990338-2; https://dx.doi.org/10.1016/0003-9861%2879%2990338-2
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know