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Escherichia coli alkaline phosphatase. Relaxation spectra of ligand binding

The temperature-jump technique was used to study the binding equilibrium between the Escherichia coli alkaline phosphatase dimer and 2-hydroxy-5-nitrobenzyl phosphonate in 0.1m-tris buffer, pH8.0. Three partially discrete relaxations were observed, two of which could be related to the bimolecular as...

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Bibliografske podrobnosti
Glavni avtor: Halford, S. E.
Format: Artigo
Jezik:Inglês
Izdano: 1972
Teme:
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC1178432/
https://ncbi.nlm.nih.gov/pubmed/4561620
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