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  Intrinsic tryptophan fluorescence of bovine liver adenosine kinase, characterization of ligand binding sites and conformational changes

El Alaoui, A., Divita, G., Maury, G., Imbach, J.-L., & Goody, R. S. (1994). Intrinsic tryptophan fluorescence of bovine liver adenosine kinase, characterization of ligand binding sites and conformational changes. European Journal of Biochemistry, 221(2), 839-846. doi:10.1111/j.1432-1033.1994.tb18798.x.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A92A-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C21D-0
Genre: Journal Article

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EurJBiochem_221_1994_839.pdf (Any fulltext), 877KB
 
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 Creators:
El Alaoui, Abdelaziz, Author
Divita, Gilles1, Author              
Maury, Georges, Author
Imbach, Jean-Louis, Author
Goody, Roger S.1, Author              
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: Bovine liver adenosine kinase is a 45-kDa monomeric protein which exhibits a characteristic intrinsic tryptophan fluorescence with a maximal excitation at 284 nm and an emission peak centered at 335 nm. A total of three tryptophan residues/molecule has been estimated by using a fluorescence titration method. Low values of Stern-Volmer quenching constants in the presence of either acrylamide or iodide (4.2 M-1 or 1.5 M-1, respectively) indicated that the tryptophan residues are relatively buried in the native molecule. Tryptophan residues also showed a high heterogeneity, with a fractional accessible fluorescence value for iodide of 0.65. The enzyme fluorescence was very sensitive to substrate binding, which induced a marked fluorescence quenching, a lower tryptophan accessibility to acrylamide and iodide, and an increase in the tryptophan heterogeneity. ADP or ATP showed a monophasic saturation curve consistent with the existence of one binding site. In contrast, adenosine and AMP gave biphasic saturation curves, suggesting the existence of at least two binding sites, with a high and a low affinity. The presence of MgCl2 increased the affinity of ATP or ADP, whereas the binding of adenosine or AMP was not affected.

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Language(s): eng - English
 Dates: 1993-12-022005-03-031994-04
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 221 (2) Sequence Number: - Start / End Page: 839 - 846 Identifier: ISSN: 0014-2956
CoNE: /journals/resource/111097776606040