PMID:14583294
| Citation |
Zhang, HR, Guo, SY, Li, L and Cai, MY (2003) Study on Escherichia coli alkaline phosphatase conformation by phosphorimetry in the presence of denaturant. Spectrochim Acta A Mol Biomol Spectrosc 59:3185-91 |
|---|---|
| Abstract |
The influence of different denaturants on the phosphorescence spectrum and lifetime decay of Escherichia coli alkaline phosphatase (AP) was investigated. Phosphorescence intensity and lifetime of tryptophan residue (Trp-109) decrease upon addition of guanidine hydrochloride, ethylene diamine tetraacetic acid, and urea or decreasing acidity. The experiments show that AP undergoes different pathways with different denaturants and that the activation energy data, DeltaS degrees (not equal) and deltaH degrees (not equal) further confirm that there is a stable intermediate state between the folded and unfolded AP states in solution. |
| Links | |
| Keywords |
Alkaline Phosphatase/chemistry; Calorimetry; Escherichia coli/enzymology; Guanidine/pharmacology; Luminescence; Protein Conformation; Protein Denaturation; Thermodynamics; Tryptophan/analysis |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.